24 ch03proteins2008
•Download as PPT, PDF•
2 likes•748 views
This document discusses proteins, which are multifunctional biomolecules that perform many essential roles in organisms. It describes the basic structure of proteins, including their composition of amino acids linked by peptide bonds to form polypeptide chains that fold into complex three-dimensional shapes defined by secondary, tertiary, and quaternary structure. The document outlines how proteins carry out functions as enzymes, structural components, carriers, signals, receptors, and more. It also explains how environmental factors can cause proteins to denature and lose their structure-based functionality.
Report
Share
Report
Share
Recommended
Nucleic Acids
DNA and RNA are nucleic acids that carry genetic information. DNA stores and transmits information through generations, while RNA assists in protein synthesis. Nucleic acids are made up of nucleotides, which consist of a sugar, phosphate group, and nitrogenous base. The bases on DNA and RNA pair up through hydrogen bonding to form the double helix structure of DNA or single strands of RNA. Polymerase enzymes are necessary to copy DNA through replication and transcribe DNA into RNA through transcription.
Proteins
Proteins are made up of chains of amino acids that form various structures which determine the protein's function. The amino acid sequence forms the primary structure. Hydrogen bonding forms regular patterns of alpha helices and beta sheets as the secondary structure. Tertiary structure is the final 3D shape from hydrophobic interactions. Some proteins have quaternary structure as complexes of multiple polypeptide chains.
Inhibition of μ-calpain; towards treatment of rheumatoid arthritis
This document summarizes research on calpain inhibition for the treatment of rheumatoid arthritis. Calpains are calcium-dependent cysteine proteases implicated in inflammatory diseases. The large subunit of μ- and m-calpains contains catalytic domains and calcium binding domains. Calpastatin inhibits activated calpains. Overactivation of calpains is associated with rheumatoid arthritis due to calcium imbalance. Newly synthesized mono-halogenated α-mercaptoacrylate derivatives potently inhibit calpains by binding calcium binding domains. This study examines the interactions of these inhibitors with the PEF(L) and PEF(S) calcium binding domains.
Inhibition of μ-calpain; towards treatment of rheumatoid arthritis (2)
1. Rheumatoid arthritis is an inflammatory disease where neutrophils migrate to sites of inflammation facilitated by the action of μ-calpain, a calcium-dependent protease. Inhibiting μ-calpain could help treat rheumatoid arthritis.
2. Monohalogenated α-mercaptoacrylates are potent and selective inhibitors of calpain that bind to the PEF(S) domain, interrupting conformational changes needed for activity. Compound 2 was shown to impair neutrophil spreading.
3. The aim of the study is to further elucidate the interactions of α-mercaptoacrylate inhibitors with calpain domains to optimize them as drug candidates for treating rheumatoid arthritis and other
Protein and Its structure
Proteins are made up of amino acids linked together through peptide bonds. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structure involves local folding into structures like alpha helices and beta sheets. Tertiary structure describes the overall 3D shape formed by interactions between amino acid side chains. Quaternary structure occurs when multiple protein subunits assemble to form an oligomeric complex.
Protein structure
Describes the structural organisation of proteins with example and its determination, interrelationship b/w structure and function of proteins, also biologically important peptides is covered.
by Dr. N. Sivaranjani, MD
Biol161 02
The document discusses the key biomolecules found in living things including proteins, carbohydrates, lipids, and nucleic acids. It describes the basic monomers like amino acids and nucleotides that make up these biomolecules, and how they are linked together through peptide bonds in proteins or phosphodiester bonds in nucleic acids. It also provides examples of specific biomolecules like collagen, hemoglobin, and fatty acids to illustrate their structures and functions.
Protein structure & function
Proteins fold into their functional three-dimensional shapes due to interactions between the amino acid side chains. The primary structure of a protein is its amino acid sequence, while secondary structures like alpha helices and beta sheets form due to hydrogen bonds within the peptide backbone. Tertiary structure is determined by non-covalent interactions between the side chains that stabilize the overall three-dimensional structure of the protein. Quaternary structure refers to the interaction between multiple polypeptide subunits in a single protein.
Recommended
Nucleic Acids
DNA and RNA are nucleic acids that carry genetic information. DNA stores and transmits information through generations, while RNA assists in protein synthesis. Nucleic acids are made up of nucleotides, which consist of a sugar, phosphate group, and nitrogenous base. The bases on DNA and RNA pair up through hydrogen bonding to form the double helix structure of DNA or single strands of RNA. Polymerase enzymes are necessary to copy DNA through replication and transcribe DNA into RNA through transcription.
Proteins
Proteins are made up of chains of amino acids that form various structures which determine the protein's function. The amino acid sequence forms the primary structure. Hydrogen bonding forms regular patterns of alpha helices and beta sheets as the secondary structure. Tertiary structure is the final 3D shape from hydrophobic interactions. Some proteins have quaternary structure as complexes of multiple polypeptide chains.
Inhibition of μ-calpain; towards treatment of rheumatoid arthritis
This document summarizes research on calpain inhibition for the treatment of rheumatoid arthritis. Calpains are calcium-dependent cysteine proteases implicated in inflammatory diseases. The large subunit of μ- and m-calpains contains catalytic domains and calcium binding domains. Calpastatin inhibits activated calpains. Overactivation of calpains is associated with rheumatoid arthritis due to calcium imbalance. Newly synthesized mono-halogenated α-mercaptoacrylate derivatives potently inhibit calpains by binding calcium binding domains. This study examines the interactions of these inhibitors with the PEF(L) and PEF(S) calcium binding domains.
Inhibition of μ-calpain; towards treatment of rheumatoid arthritis (2)
1. Rheumatoid arthritis is an inflammatory disease where neutrophils migrate to sites of inflammation facilitated by the action of μ-calpain, a calcium-dependent protease. Inhibiting μ-calpain could help treat rheumatoid arthritis.
2. Monohalogenated α-mercaptoacrylates are potent and selective inhibitors of calpain that bind to the PEF(S) domain, interrupting conformational changes needed for activity. Compound 2 was shown to impair neutrophil spreading.
3. The aim of the study is to further elucidate the interactions of α-mercaptoacrylate inhibitors with calpain domains to optimize them as drug candidates for treating rheumatoid arthritis and other
Protein and Its structure
Proteins are made up of amino acids linked together through peptide bonds. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structure involves local folding into structures like alpha helices and beta sheets. Tertiary structure describes the overall 3D shape formed by interactions between amino acid side chains. Quaternary structure occurs when multiple protein subunits assemble to form an oligomeric complex.
Protein structure
Describes the structural organisation of proteins with example and its determination, interrelationship b/w structure and function of proteins, also biologically important peptides is covered.
by Dr. N. Sivaranjani, MD
Biol161 02
The document discusses the key biomolecules found in living things including proteins, carbohydrates, lipids, and nucleic acids. It describes the basic monomers like amino acids and nucleotides that make up these biomolecules, and how they are linked together through peptide bonds in proteins or phosphodiester bonds in nucleic acids. It also provides examples of specific biomolecules like collagen, hemoglobin, and fatty acids to illustrate their structures and functions.
Protein structure & function
Proteins fold into their functional three-dimensional shapes due to interactions between the amino acid side chains. The primary structure of a protein is its amino acid sequence, while secondary structures like alpha helices and beta sheets form due to hydrogen bonds within the peptide backbone. Tertiary structure is determined by non-covalent interactions between the side chains that stabilize the overall three-dimensional structure of the protein. Quaternary structure refers to the interaction between multiple polypeptide subunits in a single protein.
Protein structure classification
This document discusses protein structure, classification, prediction, and visualization. It covers secondary structure elements like alpha helices and beta sheets, as well as tertiary and quaternary structure. It describes protein structure databases like the Protein Data Bank and tools for visualizing protein structures. Different amino acid properties that influence secondary structure are also discussed.
Proteins basics
This document discusses the primary, secondary, tertiary, and quaternary structure of proteins. It begins by describing the important biological functions of proteins and the general structures of globular and fibrous proteins. It then discusses the structures of amino acids and how peptide bonds link amino acids into polypeptide chains. The levels of protein structure are introduced, including the alpha helix and beta sheet secondary structures, tertiary folding of polypeptide chains, and arrangement of subunits in quaternary structure. Common protein domains and motifs are also illustrated.
Proteins
Proteins have many important functions in the body including structure, catalysis, movement, transport, hormones, protection, storage, and regulation. They are composed of amino acids that are linked together through peptide bonds to form polypeptide chains or folded structures. The structure of proteins includes primary, secondary, tertiary, and sometimes quaternary levels that determine the protein's shape and function. Denaturation can disrupt a protein's structure through physical or chemical means.
Protein structure
Proteins are composed of amino acids bonded together in chains called polypeptides. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the sequence of amino acids in the polypeptide chain. The secondary structure describes local folding patterns like alpha helices and beta sheets formed by hydrogen bonds. Tertiary structure refers to the overall 3D shape formed by interactions between amino acids distant in the chain. Quaternary structure involves the interaction of multiple polypeptide chains. Changes in protein structure can alter its function.
Protein
Different structure of proteins and the classifications according to it .Explanation with structure and arranges in sequence
Introduction to protein and classification by sohail
This document provides an introduction and overview of protein structure and classification. It discusses the basic building blocks of proteins, the four levels of protein structure (primary, secondary, tertiary, and quaternary), and two main methods of protein classification - by shape (globular vs. fibrous proteins) and by function (enzymes, hormones, structural proteins, etc.). The document aims to cover key concepts about protein structure and organization in a comprehensive yet concise manner.
Protein structural organisation
Proteins play key roles in living systems through catalysis, transport, and information transfer. They have a hierarchical structure including primary, secondary, tertiary, and quaternary levels. The primary structure is the amino acid sequence, and higher levels of organization are determined by the primary structure. Protein folding and interactions between residues determine the final 3D tertiary and quaternary structures, which are critical for protein function. Misfolded proteins can cause diseases.
Part I : Introduction to Protein Structure
This document provides an overview of protein structure, including levels of structure and classification. It discusses the importance of protein structure in determining function. The primary levels of structure are defined as primary (amino acid sequence), secondary (local folding patterns like alpha helices and beta sheets), tertiary (packing of secondary structures), and quaternary (assembly of protein chains). Protein structures can be classified based on their secondary structure composition as all-alpha, all-beta, alpha/beta, or alpha+beta. Domains are compact folding units associated with function.
IB Proteins & Enzymes Review (2.4-2.5-7.3)
This document contains review questions for a biology exam on proteins and enzymes. It includes questions about protein structure, functions of different protein types, enzyme structure and function, and the effects of temperature, pH and substrate concentration on enzyme activity. Specific review questions cover topics like protein denaturation, enzyme specificity, and the industrial production of lactose-free milk.
Phys 02 13
There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids in the polypeptide chain. The secondary structure involves hydrogen bonds forming coils, sheets, or loops. Tertiary structure is the packing of these secondary structures into domains. Quaternary structure involves multiple proteins combining. A protein's shape determines its function, and denaturation can destroy this shape and impair function.
Protein folding
The document discusses protein folding, which is the process by which a polypeptide chain folds into its characteristic and functional three-dimensional structure. It describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. Key drivers of folding are the hydrophobic effect and formation of hydrogen bonds. Chaperone proteins assist in protein folding in vivo. Factors such as mutations, errors in synthesis, environmental stresses, and aging can cause proteins to misfold and aggregate, which is associated with various diseases. Cells use molecular chaperones and protein degradation systems to prevent aggregation, but these become less effective with age.
Protein Folding Mechanism
Folding depends upon sequence of Amino Acids not the Composition. Folding starts with the secondary structure and ends at quaternary structure.
Denaturation occur at secondary, tertiary & quaternary level but not at primary level.
Protein structure
The document summarizes the structure of proteins at different levels:
- Primary structure is the specific sequence of amino acids in the protein backbone.
- Secondary structure describes segments of the backbone chain forming regular structures like alpha helices or beta pleated sheets.
- Tertiary structure is the overall 3D shape of the protein formed by interactions between amino acid side chains.
- Quaternary structure refers to proteins with multiple polypeptide chains interacting to form a complex.
Presentation1
This document discusses the structure and functions of proteins and nucleic acids. It provides details on the primary, secondary, tertiary, and quaternary structure of proteins. It also describes the basic components and double helix structure of DNA and RNA. The key roles of DNA in storing genetic information and RNA in synthesizing proteins are summarized.
STRUCTURAL ORGANIZATION OF PROTEINS
Primary structure of protein
Secondary structure of protein
Tertiary structure of protein
Quaternary structure of protein
Methods to determine protein structure
Conclusion
References
METHODS TO DETERMINE PROTEIN STRUCTURE
Each protein has a unique sequence of amino acids.
The amino acids are held together in a protein by
covalent peptide bonds or linkages.
A peptide bond are formed when amino group of an
amino acid combines with the carboxyl group of another.
The conformation of polypeptide chain by twisting or folding is referred to as secondary structure.
Two types of secondary structures α-helix and β-sheet are mainly identified.
α-Helical structure was proposed by Pauling and Corey in 1951.
It occurs when the sequence of amino acids are linked by hydrogen bonds.
Each turn of α-helix contains 3.6 amino acids.
β-pleated sheets are composed of two or more segments of fully extended peptide chains.
β-Sheets may be arranged either in parallel or anti-parallel direction.
Many globular proteins contain combinations of α-helix and β-pleated sheet secondary structure, these patterns are called supersecondary structures also called motifs.
The three dimensional arrangement of protein structure is referred to as tertiary structure.
It is a compact structure with hydrophobic side chains held interior while the hydrophilic groups are on the surface.
This type of arrangement provide stability of the molecule.
Besides the H-bongs, disulfide bonds, ionic interactions, hydrophobic interactions also contribute to the tertiary structure.
Protein Folding-biophysical and cellular aspects, protein denaturation
Protein folding is the physical process by which a protein chain acquires its native 3-dimensional structure, a conformation that is usually biologically functional, in an expeditious and reproducible manner.
Enzyme
The document discusses the classification and properties of enzymes. It states that enzymes are classified according to the type of reaction they catalyze into seven major classes by the International Union of Biochemistry and Molecular Biology (IUBMB). Each enzyme is assigned a four-digit Enzyme Commission (EC) number that defines its catalytic reaction. The document also describes enzyme mechanisms such as the formation of enzyme-substrate complexes, cofactors that enzymes require, and models of substrate binding like the lock-and-key and induced fit models.
Protein structure, Protein unfolding and misfolding
Protein structure- Four levels of the organization of protein structure; Primary, secondary, tertiary and quaternary protein structure.
Pro fold
This document discusses protein folding in the cell. It begins by introducing cellular compartments and the concept of molecular crowding in the cytosol. It then discusses co-translational folding, where proteins begin folding as they are synthesized on the ribosome. Molecular chaperones are introduced as proteins that assist other proteins to properly fold and assemble in the cell. Examples are given of intramolecular and chemical chaperones that can stabilize proteins. The effects of molecular crowding in increasing protein association are also summarized.
Polypeptides of defined sequence
Proteins are polypeptides with a defined sequence of amino acids. Each protein's sequence is determined by instructions contained in the cell's genetic material, which specifies which of the 20 standard amino acids make up the protein and in what order. This precise sequence defines the protein's structure and function.
Water potential practice questions
This document contains 7 sample questions about water potential (Ψ). The questions ask students to calculate Ψ values based on given information about solute potential (Ψs) and pressure potential (Ψp). They also ask students to determine the direction of water flow between solutions and plant cells based on their relative water potentials. The questions cover core concepts in calculating and applying water potential.
Genetics ppt chap.14
This document contains 51 questions about genetics concepts including:
- Gregor Mendel's experiments with pea plants and the laws of segregation and independent assortment he discovered.
- Basic genetics terminology such as alleles, genotypes, phenotypes, homozygous, heterozygous.
- Monohybrid and dihybrid crosses, Punnett squares, and probability.
- Exceptions and expansions on Mendel's work including incomplete dominance, codominance, sex-linked traits.
- Human genetics concepts like pedigrees, inherited diseases and their ethnic distributions.
More Related Content
What's hot
Protein structure classification
This document discusses protein structure, classification, prediction, and visualization. It covers secondary structure elements like alpha helices and beta sheets, as well as tertiary and quaternary structure. It describes protein structure databases like the Protein Data Bank and tools for visualizing protein structures. Different amino acid properties that influence secondary structure are also discussed.
Proteins basics
This document discusses the primary, secondary, tertiary, and quaternary structure of proteins. It begins by describing the important biological functions of proteins and the general structures of globular and fibrous proteins. It then discusses the structures of amino acids and how peptide bonds link amino acids into polypeptide chains. The levels of protein structure are introduced, including the alpha helix and beta sheet secondary structures, tertiary folding of polypeptide chains, and arrangement of subunits in quaternary structure. Common protein domains and motifs are also illustrated.
Proteins
Proteins have many important functions in the body including structure, catalysis, movement, transport, hormones, protection, storage, and regulation. They are composed of amino acids that are linked together through peptide bonds to form polypeptide chains or folded structures. The structure of proteins includes primary, secondary, tertiary, and sometimes quaternary levels that determine the protein's shape and function. Denaturation can disrupt a protein's structure through physical or chemical means.
Protein structure
Proteins are composed of amino acids bonded together in chains called polypeptides. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the sequence of amino acids in the polypeptide chain. The secondary structure describes local folding patterns like alpha helices and beta sheets formed by hydrogen bonds. Tertiary structure refers to the overall 3D shape formed by interactions between amino acids distant in the chain. Quaternary structure involves the interaction of multiple polypeptide chains. Changes in protein structure can alter its function.
Protein
Different structure of proteins and the classifications according to it .Explanation with structure and arranges in sequence
Introduction to protein and classification by sohail
This document provides an introduction and overview of protein structure and classification. It discusses the basic building blocks of proteins, the four levels of protein structure (primary, secondary, tertiary, and quaternary), and two main methods of protein classification - by shape (globular vs. fibrous proteins) and by function (enzymes, hormones, structural proteins, etc.). The document aims to cover key concepts about protein structure and organization in a comprehensive yet concise manner.
Protein structural organisation
Proteins play key roles in living systems through catalysis, transport, and information transfer. They have a hierarchical structure including primary, secondary, tertiary, and quaternary levels. The primary structure is the amino acid sequence, and higher levels of organization are determined by the primary structure. Protein folding and interactions between residues determine the final 3D tertiary and quaternary structures, which are critical for protein function. Misfolded proteins can cause diseases.
Part I : Introduction to Protein Structure
This document provides an overview of protein structure, including levels of structure and classification. It discusses the importance of protein structure in determining function. The primary levels of structure are defined as primary (amino acid sequence), secondary (local folding patterns like alpha helices and beta sheets), tertiary (packing of secondary structures), and quaternary (assembly of protein chains). Protein structures can be classified based on their secondary structure composition as all-alpha, all-beta, alpha/beta, or alpha+beta. Domains are compact folding units associated with function.
IB Proteins & Enzymes Review (2.4-2.5-7.3)
This document contains review questions for a biology exam on proteins and enzymes. It includes questions about protein structure, functions of different protein types, enzyme structure and function, and the effects of temperature, pH and substrate concentration on enzyme activity. Specific review questions cover topics like protein denaturation, enzyme specificity, and the industrial production of lactose-free milk.
Phys 02 13
There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids in the polypeptide chain. The secondary structure involves hydrogen bonds forming coils, sheets, or loops. Tertiary structure is the packing of these secondary structures into domains. Quaternary structure involves multiple proteins combining. A protein's shape determines its function, and denaturation can destroy this shape and impair function.
Protein folding
The document discusses protein folding, which is the process by which a polypeptide chain folds into its characteristic and functional three-dimensional structure. It describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. Key drivers of folding are the hydrophobic effect and formation of hydrogen bonds. Chaperone proteins assist in protein folding in vivo. Factors such as mutations, errors in synthesis, environmental stresses, and aging can cause proteins to misfold and aggregate, which is associated with various diseases. Cells use molecular chaperones and protein degradation systems to prevent aggregation, but these become less effective with age.
Protein Folding Mechanism
Folding depends upon sequence of Amino Acids not the Composition. Folding starts with the secondary structure and ends at quaternary structure.
Denaturation occur at secondary, tertiary & quaternary level but not at primary level.
Protein structure
The document summarizes the structure of proteins at different levels:
- Primary structure is the specific sequence of amino acids in the protein backbone.
- Secondary structure describes segments of the backbone chain forming regular structures like alpha helices or beta pleated sheets.
- Tertiary structure is the overall 3D shape of the protein formed by interactions between amino acid side chains.
- Quaternary structure refers to proteins with multiple polypeptide chains interacting to form a complex.
Presentation1
This document discusses the structure and functions of proteins and nucleic acids. It provides details on the primary, secondary, tertiary, and quaternary structure of proteins. It also describes the basic components and double helix structure of DNA and RNA. The key roles of DNA in storing genetic information and RNA in synthesizing proteins are summarized.
STRUCTURAL ORGANIZATION OF PROTEINS
Primary structure of protein
Secondary structure of protein
Tertiary structure of protein
Quaternary structure of protein
Methods to determine protein structure
Conclusion
References
METHODS TO DETERMINE PROTEIN STRUCTURE
Each protein has a unique sequence of amino acids.
The amino acids are held together in a protein by
covalent peptide bonds or linkages.
A peptide bond are formed when amino group of an
amino acid combines with the carboxyl group of another.
The conformation of polypeptide chain by twisting or folding is referred to as secondary structure.
Two types of secondary structures α-helix and β-sheet are mainly identified.
α-Helical structure was proposed by Pauling and Corey in 1951.
It occurs when the sequence of amino acids are linked by hydrogen bonds.
Each turn of α-helix contains 3.6 amino acids.
β-pleated sheets are composed of two or more segments of fully extended peptide chains.
β-Sheets may be arranged either in parallel or anti-parallel direction.
Many globular proteins contain combinations of α-helix and β-pleated sheet secondary structure, these patterns are called supersecondary structures also called motifs.
The three dimensional arrangement of protein structure is referred to as tertiary structure.
It is a compact structure with hydrophobic side chains held interior while the hydrophilic groups are on the surface.
This type of arrangement provide stability of the molecule.
Besides the H-bongs, disulfide bonds, ionic interactions, hydrophobic interactions also contribute to the tertiary structure.
Protein Folding-biophysical and cellular aspects, protein denaturation
Protein folding is the physical process by which a protein chain acquires its native 3-dimensional structure, a conformation that is usually biologically functional, in an expeditious and reproducible manner.
Enzyme
The document discusses the classification and properties of enzymes. It states that enzymes are classified according to the type of reaction they catalyze into seven major classes by the International Union of Biochemistry and Molecular Biology (IUBMB). Each enzyme is assigned a four-digit Enzyme Commission (EC) number that defines its catalytic reaction. The document also describes enzyme mechanisms such as the formation of enzyme-substrate complexes, cofactors that enzymes require, and models of substrate binding like the lock-and-key and induced fit models.
Protein structure, Protein unfolding and misfolding
Protein structure- Four levels of the organization of protein structure; Primary, secondary, tertiary and quaternary protein structure.
Pro fold
This document discusses protein folding in the cell. It begins by introducing cellular compartments and the concept of molecular crowding in the cytosol. It then discusses co-translational folding, where proteins begin folding as they are synthesized on the ribosome. Molecular chaperones are introduced as proteins that assist other proteins to properly fold and assemble in the cell. Examples are given of intramolecular and chemical chaperones that can stabilize proteins. The effects of molecular crowding in increasing protein association are also summarized.
Polypeptides of defined sequence
Proteins are polypeptides with a defined sequence of amino acids. Each protein's sequence is determined by instructions contained in the cell's genetic material, which specifies which of the 20 standard amino acids make up the protein and in what order. This precise sequence defines the protein's structure and function.
What's hot (20)
Introduction to protein and classification by sohail
Introduction to protein and classification by sohail
Protein Folding-biophysical and cellular aspects, protein denaturation
Protein Folding-biophysical and cellular aspects, protein denaturation
Protein structure, Protein unfolding and misfolding
Protein structure, Protein unfolding and misfolding
Viewers also liked
Water potential practice questions
This document contains 7 sample questions about water potential (Ψ). The questions ask students to calculate Ψ values based on given information about solute potential (Ψs) and pressure potential (Ψp). They also ask students to determine the direction of water flow between solutions and plant cells based on their relative water potentials. The questions cover core concepts in calculating and applying water potential.
Genetics ppt chap.14
This document contains 51 questions about genetics concepts including:
- Gregor Mendel's experiments with pea plants and the laws of segregation and independent assortment he discovered.
- Basic genetics terminology such as alleles, genotypes, phenotypes, homozygous, heterozygous.
- Monohybrid and dihybrid crosses, Punnett squares, and probability.
- Exceptions and expansions on Mendel's work including incomplete dominance, codominance, sex-linked traits.
- Human genetics concepts like pedigrees, inherited diseases and their ethnic distributions.
Chi squarepractice
This document provides examples of chi square practice problems involving genetic crosses in fruit flies and chickens. For each problem, it gives the expected genotypes and observed results, calculates the chi square value to determine if it supports or rejects the given hypotheses, and provides the chi square answers. It also includes explanations of how to set up and solve chi square problems to test hypotheses about inheritance patterns.
Unit 2 at a glance - new curriculum
This unit covers the chemistry of life over 12 days. Students will read chapters 1-6 or 8 in the textbook. Key topics include hypotheses of the origin of life, organisms requiring constant energy input and matter exchange, and how the subcomponents and sequence of biological molecules determine their properties and structure/function. Students will perform a lab on the effect of various factors on enzyme activity. Formulas for Gibbs free energy will also be covered. Assessment will include a traditional test with an essay question and multiple choice, addressing topics like controlled experiments, bonding types, water properties, carbon bonding, macromolecule structure/function, metabolism, and regulation of enzymes.
Macromolecule chapter 5 practice
This document appears to be an answer key for a practice test on macromolecules. It lists macromolecule chapter 5 practice questions and their answers, with the answers being the type of macromolecule that corresponds to each question - proteins, lipids, carbohydrates, or nucleic acids. There are 45 questions total and the document simply lists the question number followed by the macromolecule that is the answer key for that question.
Ap biology enzyme webquest
This document provides information from 10 different websites about enzymes and how they function in the body. It includes details on the structure of enzymes and their active sites, how they catalyze reactions, factors that affect their function like pH and temperature, and how enzyme inhibitors can be used as drugs. For example, it explains that aspirin works by inhibiting the cyclooxygenase enzyme pathway to reduce inflammation. It also discusses how ACE inhibitors are used to treat high blood pressure and how some antidepressants function as enzyme inhibitors in the brain.
Errors of meiosis and chromosomal abnormalities
A chromosomal abnormality occurs when there is an extra or missing chromosome, or structural changes to a chromosome. Nondisjunction during meiosis can result in an extra or missing chromosome when homologous chromosomes fail to separate properly. This can cause disorders like Down syndrome (trisomy 21), which is associated with older maternal age and causes cognitive impairment. Other disorders include Klinefelter syndrome (XXY), Jacobs syndrome (XXY), and Turner syndrome (XO), each with their own characteristics. Chromosome breakage can also cause abnormalities if fragments are lost or gained.
58 ch13beyondmendel2008
This document discusses several concepts in genetics beyond Mendel's laws of inheritance:
1) Incomplete dominance results in an intermediate phenotype in heterozygotes, such as pink flowers from a cross of red and white flowering plants.
2) Co-dominance occurs when two alleles are fully expressed in the phenotype, like the ABO blood groups in humans where the IA and IB alleles both produce antigens.
3) Pleiotropy is when one gene affects multiple phenotypic traits, such as genes for dwarfism or gigantism affecting both height and other body features.
4) Epistasis occurs when one gene masks the expression of another gene, as in coat color genes in mice or dogs.
26 ch05cellsoverview2007
This document provides an overview of cell biology concepts covered in an AP Biology course. It discusses the structures and functions of organelles such as the nucleus, mitochondria, chloroplasts, lysosomes, endoplasmic reticulum, and Golgi apparatus. It explains how cells produce proteins, make energy, digest materials, transport vesicles, and divide. The cytoskeleton and its role in maintaining cell shape, anchoring organelles, and enabling cell motion are also summarized.
Colon cancer
1. Jane receives a call from her brother Sam informing her that he has been diagnosed with colon cancer. Their father also died from colon cancer.
2. Jane visits her doctor who recommends genetic testing to determine if Jane has a genetic predisposition to colon cancer. Jane and Sam meet with a genetic counselor.
3. Genetic testing reveals that Sam has a mutation in the APC gene, which is associated with familial adenomatous polyposis (FAP), a hereditary form of colon cancer. Further testing shows Jane also has the same APC gene mutation.
Ap biology lab notebook
- The document outlines the requirements for AP Biology lab notebooks including formatting, content, and structure.
- Key requirements include using pencil, including identifying information on the cover, numbering pages, using third person, skipping lines between sections, and following specific formats for confirmation and inquiry labs.
- Sections must include the title, date, pre-lab questions, objective, materials, procedure, data, analysis, conclusion, and be written in a specific format and order.
Unit 3 cells unit at a glance new curriculum
This unit covers cell structure and function over 18 days. Students will read chapters 6-8, 11-12 from the textbook and cover topics on cellular energy and matter exchange, membrane structure and selective permeability, intercellular and intracellular signaling, subcellular components and interactions, and the cell cycle. Labs include using microscopes to observe cell structures, diffusion and osmosis, and mitosis in onion root tips. Lecture topics focus on comparing prokaryotic and eukaryotic cells, animal and plant cells, membrane properties, signal transduction pathways, and the phases of the cell cycle.
Mol bio classics
The document summarizes the classic experiment conducted by Matthew Meselson and Frank Stahl in 1958 that determined the mechanism of DNA replication. They grew bacteria in a culture containing the heavy isotope nitrogen-15 to produce "heavy" DNA. When these bacteria were then grown in a culture with regular nitrogen-14, the resulting DNA had an intermediate density, indicating that DNA replicates semiconservatively, with each parent strand serving as a template to produce two daughter double helices. Subsequent experiments showed that after a second generation, the DNA was half heavy and half light, confirming the semiconservative model. This elegant experiment provided the first direct evidence that DNA replicates in this manner.
Unit 7 unit at a glance
This unit covers evolution over 20 days through reading chapters 21-26 in the textbook. It focuses on key concepts like natural selection acting on phenotypic variations, evolutionary change driven by random processes, and evidence for evolution from fields like mathematics. Students will learn about speciation, extinction, phylogenetic trees, and hypotheses for the origin of life on Earth. Labs include using Hardy-Weinberg calculations to model evolution and using bioinformatics to analyze DNA sequences and evolutionary relationships. The chapters cover topics such as gene expression and development, Darwin's theory of evolution by natural selection, population genetics, speciation mechanisms, phylogeny, and the development of life on Earth.
Chemistry review
1. This document provides a review of basic chemistry concepts that AP Biology students should already be familiar with, including: the symbols and charges of common elements, molecular and structural formulas, molarity calculations, water properties, pH, buffers, isomers and functional groups.
2. Students are instructed to add this review material to their AP Biology binder for reference. The review covers topics like atomic structure, compounds, solutions, acid-base chemistry and organic chemistry basics.
3. Examples of important concepts highlighted are water's polar nature and how it relates to biological phenomena, the importance of small pH changes in living systems, what buffers are and how they function in organisms, and why carbon is the central atom in
Midterm grid in exercises(students)
Here are the steps to perform a chi-square analysis on the given data:
1) Set up a contingency table with the observed and expected frequencies:
Phenotype Observed Expected
White eyes (ww) 210 225
Wild type eyes (WW and Ww) 680 675
Total 890 900
2) Calculate the chi-square value:
Chi-square = Σ(Observed - Expected)^2/Expected
= (210-225)^2/225 + (680-675)^2/675 = 0.44
3) Determine the degrees of freedom (df):
df = (number of rows - 1) x (number of columns - 1)
56 ch15chromosomalabnormalities2008
This document discusses chromosomal abnormalities that can occur due to errors in meiosis, including nondisjunction where chromosomes do not separate properly, leading to an incorrect number of chromosomes. Specific abnormalities are described such as Down syndrome, which results from trisomy 21 where a person has three copies of chromosome 21. Other sex chromosome abnormalities are also summarized like Klinefelter syndrome, Turner syndrome, and Jacob's syndrome. The document provides information on the frequency of these disorders and their characteristic symptoms.
Making energy ppt questions chap9
Organisms need energy to sustain life processes like growth, movement, and reproduction. They obtain energy primarily from food sources through cellular respiration. Cellular respiration involves glycolysis, the Krebs cycle, and the electron transport chain to break down glucose and harvest energy, producing ATP as energy currency. ATP is an excellent energy donor that is recycled thousands of times per second to power cellular work. The three main stages of cellular respiration extract energy from glucose in steps, with glycolysis occurring in the cytoplasm, the Krebs cycle in the mitochondrial matrix, and the electron transport chain across the inner mitochondrial membrane via chemiosmosis. Oxygen is required for the electron transport chain, which produces the most ATP and drives ATP synthesis. Cellular
36 ch09respiration42008
The document summarizes cellular respiration and how it uses the electron transport chain (ETC) in the mitochondria to produce ATP from glucose. It explains that glycolysis and the Krebs cycle produce a small amount of ATP, but the ETC is needed to extract much more energy. The ETC uses protein complexes to transport electrons and pump hydrogen ions across the inner mitochondrial membrane. This builds a proton gradient that is used by ATP synthase to produce large amounts of ATP through oxidative phosphorylation. In total, glucose broken down aerobically by cellular respiration can yield around 36 ATP molecules through this process.
23 ch03lipids2008
This document discusses lipids, including their structure and functions. Lipids are composed of carbon, hydrogen, and oxygen and include fats, phospholipids, and steroids. Fats are composed of glycerol bonded to fatty acids through dehydration synthesis. Phospholipids have a hydrophilic phosphate head and hydrophobic fatty acid tails, allowing them to form bilayers that serve as cell membranes. Cholesterol is an important component of cell membranes and can be converted into sex hormones.
Viewers also liked (20)
Similar to 24 ch03proteins2008
Proteins
This document discusses proteins, which are complex biomolecules that perform a wide variety of essential functions in organisms. Proteins are made up of amino acid monomers that join together via peptide bonds to form polypeptide chains. The sequence and interactions of amino acid side chains determine a protein's unique 3D structure at the primary, secondary, tertiary, and sometimes quaternary levels. This complex structure is essential for a protein's specific functions, such as catalyzing reactions as enzymes, transporting molecules, or providing structure. Environmental factors can cause proteins to denature by disrupting bonds and changing shape, destroying their normal functions.
Proteins
Proteins are the most structurally and functionally diverse molecules in biology. They perform many important functions through their unique three-dimensional structures, which are determined by their sequences of amino acids. The 20 types of amino acids vary in properties like polarity and hydrophobicity, allowing proteins to fold into complex shapes. Changes in a protein's amino acid sequence or structure can significantly impact its function in the cell.
Biochem PROTEINS.pdf
This document provides information about proteins including their structure, functions, and classification. It discusses that proteins are the most structurally and functionally diverse biomolecules, accounting for over 50% of dry cell mass. They are involved in many functions including metabolism, storage, support, transport, regulation, and motion. The document describes the building blocks of proteins as amino acids and explains the four levels of protein structure: primary, secondary, tertiary, and quaternary. It also lists some examples of structural and functional proteins.
biochemistry ppt 3 by Sohail Riaz.pptx
This document summarizes key topics in protein biochemistry, including:
- The 20 amino acids that make up proteins and their classification.
- The four levels of protein structure: primary, secondary, tertiary, and quaternary.
- Common protein functions in metabolism, structure, transport, defense, regulation, and motion.
- Enzyme structure and function, including active sites and factors that affect enzyme activity such as temperature, pH, and inhibitors.
- The mechanisms of enzyme action including lock-and-key and induced fit models.
- Different types of enzyme inhibition such as competitive, non-competitive, and uncompetitive inhibition.
STUDENT PPT.pdf
This document provides information about biomolecules called proteins. It discusses that proteins are multifunctional molecules that are involved in metabolism, support, transport, regulation, motion and defense. It describes the structure of proteins including that they are made up of amino acid monomers that form polypeptide chains. The chains fold into complex 3D shapes determined by primary, secondary, tertiary and sometimes quaternary structure. This folding allows proteins to perform diverse functions in the body such as acting as enzymes, hormones, antibodies and structural components of tissues.
Protein
Protein are essential nutrients for the human body They are one of the building blocks of body tissue and can also serve as a fuel source. As a fuel, proteins provide as much energy density as carbohydrates: 4 kcal (17 kJ) per gram; in contrast, lipids provide 9 kcal (37 kJ) per gram. The most important aspect and defining characteristic of proteins from a nutritional standpoint is its amino acid composition.
For more information click on the link: http://fitness100.rf.gd/protein/
Amino Acids and Protein
Study Material for B.Sc. Students
Primary, secondary, tertiary, quaternary structures of protein, motiffs and domains, subunits
ch 3 proteins student print.pptx
Proteins are multifunctional biomolecules that perform nearly every function in living organisms. They have complex three-dimensional structures determined by their amino acid sequences that allow them to serve critical roles including metabolism, structure, transport, defense, regulation, and motion. Proteins fold into complex shapes through interactions between their amino acid side chains that enable them to carry out diverse and essential functions in the body.
Proteins and Amino Acids
Proteins are composed of amino acids and have four levels of structure - primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Common secondary structures include alpha helices and beta pleated sheets formed by hydrogen bonding. Tertiary structure describes the overall 3D shape formed by interactions between amino acid side chains. Globular proteins fold such that hydrophobic residues are buried inside and hydrophilic residues face outward, while fibrous proteins form insoluble fibers.
Proteins
Proteins are made up of amino acids linked together by peptide bonds. The specific sequence and 3D structure of a protein determines its function. There are four levels of protein structure: primary structure is the amino acid sequence; secondary structure includes alpha helices and beta sheets from hydrogen bonding; tertiary structure is the overall folded shape from various weak interactions; and quaternary structure involves multiple protein subunits interacting.
Organic compounds presentation
This document provides an overview of organic compounds and macromolecules. It discusses the four major classes of macromolecules - carbohydrates, lipids, proteins, and nucleic acids. For each class, it describes the monomer units, examples, functions, and how the monomers polymerize to form larger molecules through condensation reactions. It also covers topics like DNA replication, protein structure and folding, and the roles of these macromolecules in biological processes.
AMINO ACID & PROTEIN CHEMISTRY.pptx
this ppt covers about amino acids, classification, protein ,classifications, structure, denaturation, structure & fnctional relationship with applied aspects.
ch 3 proteins structure ppt.ppt
Proteins are multifunctional biomolecules that perform diverse roles in the body. They are involved in metabolism, structure and support, transport, regulation, and motion. Proteins are made of amino acid monomers that join together via peptide bonds to form polypeptide chains which fold into complex three-dimensional shapes dictated by their primary, secondary, tertiary, and sometimes quaternary structures. A protein's structure determines its specific function, such as enzymes catalyzing reactions, collagen providing structure, or hemoglobin transporting oxygen.
ch 3 proteins structure ppt.ppt
Proteins are multifunctional biomolecules that perform many essential roles in the body. They are involved in metabolism, structure and support, transport, regulation, and motion. Proteins are made of amino acid monomers that join together via peptide bonds to form complex three-dimensional shapes defined by their primary, secondary, tertiary, and sometimes quaternary structures. A protein's structure determines its specific function, such as enzymatic catalysis, mechanical support, oxygen transport, or hormonal signaling.
Proteins
Proteins are made up of chains of amino acids that form various structures which determine the protein's function. The amino acid sequence forms the primary structure. Hydrogen bonding forms regular patterns of alpha helices and beta sheets as the secondary structure. Tertiary structure is the final 3D shape from hydrophobic interactions. Some proteins have quaternary structure as complexes of multiple polypeptide chains.
The chemical nature of the cell
The document summarizes the key components that make up cells. It describes the five major classes of molecules that cells are made of: water, carbohydrates, lipids, proteins, and nucleic acids. Each class is comprised of smaller molecules that serve important functions. For example, carbohydrates include simple sugars, complex starches and structural cellulose. Lipids encompass fats, oils, and phospholipids that make up cell membranes. Proteins have complex structures and serve as enzymes, hormones, and structures. Nucleic acids like DNA and RNA contain the cell's genetic code.
Protein structure
Proteins are polymers made up of amino acid chains that form specific structures. There are four levels of protein structure:
1. Primary structure is the amino acid sequence.
2. Secondary structures include alpha helices and beta sheets formed by hydrogen bonds between amino acids.
3. Tertiary structure is the three dimensional folding of secondary structures.
4. Quaternary structure occurs in proteins made of multiple polypeptide chains that aggregate. The document discusses these levels of structure in detail, focusing on alpha helices and beta sheets as common secondary structures stabilized by hydrogen bonding.
Proteins lecture 11
This document discusses the structure of proteins at multiple levels:
1. It describes the primary structure of proteins as the unique sequence of amino acids determined by genes. The peptide bond links amino acids and is rigid and planar.
2. Secondary structures like alpha helices and beta sheets form due to hydrogen bonding between amino acids in close proximity in the sequence. Alpha helices are tightly coiled and stabilized by hydrogen bonds between amino and carbonyl groups.
3. Tertiary structure refers to the compact three-dimensional folding of the protein chain, bringing hydrophobic residues inwards and hydrophilic outwards. Disulfide bonds and other interactions contribute to tertiary structure.
4. Some proteins have quaternary structure
Protein metabolism and nitrogen fixation and metabolism
- The document discusses protein metabolism and nitrogen fixation. It covers the classification of proteins based on their structure, composition, and functions. There are four levels of protein structure - primary, secondary, tertiary, and quaternary.
- The primary structure is the linear sequence of amino acids. The secondary structure involves folding into alpha helices or beta sheets via hydrogen bonding. Tertiary structure describes the overall 3D shape formed by interactions between amino acid R groups. Quaternary structure applies to proteins with multiple polypeptide chains that combine to form complexes.
- Proteins are classified as globular, fibrous, or intermediate based on their shape. They can also be simple or conjugated based on composition
@Food ppt.ppt
Proteins are composed of amino acids that are linked together by peptide bonds. They serve many important functions in the body and in foods. Proteins have complex structures including primary, secondary, tertiary, and sometimes quaternary structures that determine their shape and functionality. The structures of proteins can be altered through processes like denaturation, affecting properties like solubility. Foods contain different types of proteins that influence properties like hydration, structure formation, and interactions at surfaces.
Similar to 24 ch03proteins2008 (20)
Protein metabolism and nitrogen fixation and metabolism
Protein metabolism and nitrogen fixation and metabolism
More from sbarkanic
Physical science final exam review
This document provides a review for a Physical Science final exam, outlining 9 competencies covered on the exam. It includes 75 multiple choice and short answer questions testing understanding of concepts in motion, waves, electricity, thermodynamics, atomic structure, nuclear processes, bonding, and acids/bases. Sample questions assess knowledge of the scientific method, graphing, Newton's laws, energy transformations, electromagnetic radiation, the periodic table, nuclear reactions, and chemical equations.
Newton
This document provides 42 multi-part physics problems involving Newton's laws of motion. The problems cover concepts such as force, mass, acceleration, weight, and their relationships. Some sample answers are provided. The problems involve calculating unknown values like force, mass, or acceleration given information about real-world scenarios involving objects in motion or at rest under the influence of various forces.
Waves
1. This document discusses different types of waves including transverse, longitudinal, and electromagnetic waves. It defines key wave properties such as amplitude, wavelength, frequency, period, and wave speed.
2. Frequency is defined as the number of vibrations per second, measured in Hertz (Hz). Period is the time for one full vibration. Frequency and period are inversely related.
3. Examples are provided to demonstrate calculating wave properties like frequency, period, wavelength, and wave speed from information given about the wave.
Electric power
This document discusses electrical power and energy. It explains that power is calculated as current multiplied by voltage, and is measured in watts. It asks the reader to calculate the power needed to operate a clock radio drawing 0.05 amps from a household circuit. The document also explains that electrical energy is provided by power companies and sold to homeowners in units of kilowatt-hours, which is 1000 watts delivered for one hour. It provides an example of calculating the electrical energy used and cost for a 1200W toaster oven used for 15 minutes.
Ac dc and circuits
This document explains the differences between alternating current (AC) and direct current (DC). It defines AC as an electric current that periodically reverses direction and changes its magnitude continuously with time in contrast to DC, which flows in one direction. The document also outlines the key characteristics of series and parallel electric circuits. Series circuits have the same current flowing through all elements and the total voltage is divided among the elements. Parallel circuits have the same voltage across each element and the total current is the sum of the currents in the individual branches. The document concludes by noting that fuses are used to prevent circuit overloading by melting and breaking the circuit if too much current passes through.
Ohm's law worksheet ccp
This document provides an Ohm's Law worksheet with 6 practice problems calculating voltage, current, and resistance using the equations: I = V/R, R = V/I, and V = IR. Students are asked to use these equations to find the missing value in each circuit scenario, such as calculating the voltage applied to a light bulb with a known current and resistance.
Ohm's law's calculations
This document contains a worksheet on Ohm's Law with 14 problems. The worksheet provides the three forms of Ohm's Law and asks students to calculate values like voltage, current, and resistance using circuits with resistors and batteries. Students are asked to determine unknown values, total resistances, and currents in various circuit diagrams applying the relationships defined by Ohm's Law.
Ohm's law worksheet ccp
This document provides an Ohm's Law worksheet with 6 practice problems calculating voltage, current, and resistance using the equations: I = V/R, R = V/I, and V = IR. Students are asked to use these equations to find the missing value in each circuit scenario, such as calculating the voltage applied to a light bulb with a known current and resistance.
Ohm's law
This document discusses resistance and Ohm's Law. It describes the key parts of Ohm's Law including volts, amps, and resistance. It also explains how to calculate an unknown value using two known values and Ohm's Law. Examples are provided to demonstrate calculating current and resistance using Ohm's Law. The document also discusses how resistance affects current and electric shock, and provides examples of calculating current through the body at different resistances and voltages.
Static electricity and electrical currants
This document defines static electricity and current electricity. It explains that static electricity is caused by an imbalance of electric charges, usually through rubbing materials together, while current electricity involves the controlled flow of electrons. It distinguishes conductors that allow electron flow from insulators that do not, and describes how static charges build up and arc in lightning.
Acid bases and nuclear review sheet
This document covers acids and bases, including definitions, properties, examples and the pH scale. It also discusses acid rain, its effects and causes. For radioactivity, it defines different types and compares the strong force to the electric force in alpha and beta equations. It explains transmutation, half-life, fission and chain reactions. Additionally, it outlines nuclear power plants, how they create electricity from fission, reasons for past meltdowns and pros and cons of nuclear power. Finally, it addresses the big bang theory, evidence supporting it, the potential end of the universe, star formation, star types and life cycles.
Chemical reactions
This document discusses chemical equations and reactions. It explains that chemical equations are used to represent chemical reactions, and that they consist of reactants on the left side of the arrow yielding products on the right. It also describes how to balance chemical equations by adjusting coefficients so that the same number of each type of atom is on both sides of the equation. Balancing chemical equations ensures conservation of mass during chemical reactions.
Naming and writing compounds and molecules
This document provides instructions for writing formulas and naming ionic compounds, covalent molecules, and polyatomic ions. It explains that for ionic compounds, you write the symbols of the ions and use the crossover method to determine subscripts before naming the compound by writing the cation name followed by the anion name with "ide." For covalent molecules, Greek prefixes indicate subscripts and the name is written by specifying each element followed by the number of atoms. Polyatomic ions are also named and included in ionic compounds by looking up their formula and charge. Examples and practice problems are provided to demonstrate the process.
Bonding practice
1) The document provides instructions for drawing Lewis structures to show ionic and covalent bonding between various elements. Students are asked to draw Lewis structures for pairs of elements, and indicate electron transfers or sharing to write chemical formulas. 2) For ionic bonds, students should draw Lewis structures, arrows to show electron transfer, charges for each ion, and chemical formulas. 3) For covalent bonds, the instructions are to draw Lewis structures, circles around shared electrons, bond structures, and chemical formulas.
Atomic spectrum
The document discusses atomic spectra and the Bohr model. It explains that atoms can absorb and emit light at specific frequencies, and this atomic spectrum acts as a fingerprint that can be used to identify elements. The Bohr model describes electrons occupying different energy shells around the nucleus, and electrons absorbing and emitting energy by jumping between shells and releasing light. The document also briefly mentions flame tests and spectroscopes as methods to observe atomic spectra.
Rutherford
Ernest Rutherford (1871-1937) was a notable British physicist and chemist who made seminal contributions to the development of the modern atomic model. Through his gold foil experiment in 1911, Rutherford was able to formulate the Rutherford model of the atom, which established that atoms have a small, positively charged nucleus surrounded by low-mass electrons. For this breakthrough discovery, Rutherford received numerous honors including the Nobel Prize in Chemistry in 1908. His work fundamentally changed scientific understanding of atomic structure.
Meinter
Lise Meitner was an Austrian/German physicist born in 1878 who made significant contributions to nuclear physics. She received her doctorate in 1905 as the second woman to earn a PhD from the University of Vienna. In 1938, Meitner, Otto Hahn, and Fritz Strassmann discovered nuclear fission when bombarding uranium with neutrons. This splitting of uranium atoms led to additional neutrons and the potential for an explosive chain reaction. Sadly, her discovery was later used in 1945 for the atomic bomb dropped on Hiroshima. Meitner received several honors for her work, including the Max Planck medal in 1949.
Gell mann
Murray Gell-Mann was born in 1929 and is still living. He graduated valedictorian from Columbia Grammar School and attended Yale University at age 15. Gell-Mann won the 1969 Nobel Prize in Physics. In 1964, he discovered the quark, which makes up protons and neutrons in the nucleus. Quarks have never been isolated due to their small size of 10-15 mm. Gell-Mann is also interested in activities like bird watching and collecting antiques.
Democritus
Democritus was a Greek philosopher born around 460-457 BC in Abdera, Thrace. He developed the first atomic theory, proposing that all matter is made up of indivisible atoms moving through empty space. Democritus believed that atoms were the fundamental building blocks of the natural world and that their behavior determined natural phenomena. He and his mentor Leucippus are considered the founders of atomic theory. Democritus was highly respected in his lifetime for making discoveries and predictions that were later proven true.
More from sbarkanic (20)
Recently uploaded
Taking AI to the Next Level in Manufacturing.pdf
Read Taking AI to the Next Level in Manufacturing to gain insights on AI adoption in the manufacturing industry, such as:
1. How quickly AI is being implemented in manufacturing.
2. Which barriers stand in the way of AI adoption.
3. How data quality and governance form the backbone of AI.
4. Organizational processes and structures that may inhibit effective AI adoption.
6. Ideas and approaches to help build your organization's AI strategy.
5th LF Energy Power Grid Model Meet-up Slides
5th Power Grid Model Meet-up
It is with great pleasure that we extend to you an invitation to the 5th Power Grid Model Meet-up, scheduled for 6th June 2024. This event will adopt a hybrid format, allowing participants to join us either through an online Mircosoft Teams session or in person at TU/e located at Den Dolech 2, Eindhoven, Netherlands. The meet-up will be hosted by Eindhoven University of Technology (TU/e), a research university specializing in engineering science & technology.
Power Grid Model
The global energy transition is placing new and unprecedented demands on Distribution System Operators (DSOs). Alongside upgrades to grid capacity, processes such as digitization, capacity optimization, and congestion management are becoming vital for delivering reliable services.
Power Grid Model is an open source project from Linux Foundation Energy and provides a calculation engine that is increasingly essential for DSOs. It offers a standards-based foundation enabling real-time power systems analysis, simulations of electrical power grids, and sophisticated what-if analysis. In addition, it enables in-depth studies and analysis of the electrical power grid’s behavior and performance. This comprehensive model incorporates essential factors such as power generation capacity, electrical losses, voltage levels, power flows, and system stability.
Power Grid Model is currently being applied in a wide variety of use cases, including grid planning, expansion, reliability, and congestion studies. It can also help in analyzing the impact of renewable energy integration, assessing the effects of disturbances or faults, and developing strategies for grid control and optimization.
What to expect
For the upcoming meetup we are organizing, we have an exciting lineup of activities planned:
-Insightful presentations covering two practical applications of the Power Grid Model.
-An update on the latest advancements in Power Grid -Model technology during the first and second quarters of 2024.
-An interactive brainstorming session to discuss and propose new feature requests.
-An opportunity to connect with fellow Power Grid Model enthusiasts and users.
How to Interpret Trends in the Kalyan Rajdhani Mix Chart.pdf
A Mix Chart displays historical data of numbers in a graphical or tabular form. The Kalyan Rajdhani Mix Chart specifically shows the results of a sequence of numbers over different periods.
Introduction of Cybersecurity with OSS at Code Europe 2024
I develop the Ruby programming language, RubyGems, and Bundler, which are package managers for Ruby. Today, I will introduce how to enhance the security of your application using open-source software (OSS) examples from Ruby and RubyGems.
The first topic is CVE (Common Vulnerabilities and Exposures). I have published CVEs many times. But what exactly is a CVE? I'll provide a basic understanding of CVEs and explain how to detect and handle vulnerabilities in OSS.
Next, let's discuss package managers. Package managers play a critical role in the OSS ecosystem. I'll explain how to manage library dependencies in your application.
I'll share insights into how the Ruby and RubyGems core team works to keep our ecosystem safe. By the end of this talk, you'll have a better understanding of how to safeguard your code.
Mutation Testing for Task-Oriented Chatbots
Conversational agents, or chatbots, are increasingly used to access all sorts of services using natural language. While open-domain chatbots - like ChatGPT - can converse on any topic, task-oriented chatbots - the focus of this paper - are designed for specific tasks, like booking a flight, obtaining customer support, or setting an appointment. Like any other software, task-oriented chatbots need to be properly tested, usually by defining and executing test scenarios (i.e., sequences of user-chatbot interactions). However, there is currently a lack of methods to quantify the completeness and strength of such test scenarios, which can lead to low-quality tests, and hence to buggy chatbots.
To fill this gap, we propose adapting mutation testing (MuT) for task-oriented chatbots. To this end, we introduce a set of mutation operators that emulate faults in chatbot designs, an architecture that enables MuT on chatbots built using heterogeneous technologies, and a practical realisation as an Eclipse plugin. Moreover, we evaluate the applicability, effectiveness and efficiency of our approach on open-source chatbots, with promising results.
Programming Foundation Models with DSPy - Meetup Slides
Prompting language models is hard, while programming language models is easy. In this talk, I will discuss the state-of-the-art framework DSPy for programming foundation models with its powerful optimizers and runtime constraint system.
Your One-Stop Shop for Python Success: Top 10 US Python Development Providers
Simplify your search for a reliable Python development partner! This list presents the top 10 trusted US providers offering comprehensive Python development services, ensuring your project's success from conception to completion.
Dandelion Hashtable: beyond billion requests per second on a commodity server
This slide deck presents DLHT, a concurrent in-memory hashtable. Despite efforts to optimize hashtables, that go as far as sacrificing core functionality, state-of-the-art designs still incur multiple memory accesses per request and block request processing in three cases. First, most hashtables block while waiting for data to be retrieved from memory. Second, open-addressing designs, which represent the current state-of-the-art, either cannot free index slots on deletes or must block all requests to do so. Third, index resizes block every request until all objects are copied to the new index. Defying folklore wisdom, DLHT forgoes open-addressing and adopts a fully-featured and memory-aware closed-addressing design based on bounded cache-line-chaining. This design offers lock-free index operations and deletes that free slots instantly, (2) completes most requests with a single memory access, (3) utilizes software prefetching to hide memory latencies, and (4) employs a novel non-blocking and parallel resizing. In a commodity server and a memory-resident workload, DLHT surpasses 1.6B requests per second and provides 3.5x (12x) the throughput of the state-of-the-art closed-addressing (open-addressing) resizable hashtable on Gets (Deletes).
June Patch Tuesday
Ivanti’s Patch Tuesday breakdown goes beyond patching your applications and brings you the intelligence and guidance needed to prioritize where to focus your attention first. Catch early analysis on our Ivanti blog, then join industry expert Chris Goettl for the Patch Tuesday Webinar Event. There we’ll do a deep dive into each of the bulletins and give guidance on the risks associated with the newly-identified vulnerabilities.
Main news related to the CCS TSI 2023 (2023/1695)
An English 🇬🇧 translation of a presentation to the speech I gave about the main changes brought by CCS TSI 2023 at the biggest Czech conference on Communications and signalling systems on Railways, which was held in Clarion Hotel Olomouc from 7th to 9th November 2023 (konferenceszt.cz). Attended by around 500 participants and 200 on-line followers.
The original Czech 🇨🇿 version of the presentation can be found here: https://www.slideshare.net/slideshow/hlavni-novinky-souvisejici-s-ccs-tsi-2023-2023-1695/269688092 .
The videorecording (in Czech) from the presentation is available here: https://youtu.be/WzjJWm4IyPk?si=SImb06tuXGb30BEH .
Apps Break Data
How information systems are built or acquired puts information, which is what they should be about, in a secondary place. Our language adapted accordingly, and we no longer talk about information systems but applications. Applications evolved in a way to break data into diverse fragments, tightly coupled with applications and expensive to integrate. The result is technical debt, which is re-paid by taking even bigger "loans", resulting in an ever-increasing technical debt. Software engineering and procurement practices work in sync with market forces to maintain this trend. This talk demonstrates how natural this situation is. The question is: can something be done to reverse the trend?
Choosing The Best AWS Service For Your Website + API.pptx
Have you ever been confused by the myriad of choices offered by AWS for hosting a website or an API?
Lambda, Elastic Beanstalk, Lightsail, Amplify, S3 (and more!) can each host websites + APIs. But which one should we choose?
Which one is cheapest? Which one is fastest? Which one will scale to meet our needs?
Join me in this session as we dive into each AWS hosting service to determine which one is best for your scenario and explain why!
Driving Business Innovation: Latest Generative AI Advancements & Success Story
Are you ready to revolutionize how you handle data? Join us for a webinar where we’ll bring you up to speed with the latest advancements in Generative AI technology and discover how leveraging FME with tools from giants like Google Gemini, Amazon, and Microsoft OpenAI can supercharge your workflow efficiency.
During the hour, we’ll take you through:
Guest Speaker Segment with Hannah Barrington: Dive into the world of dynamic real estate marketing with Hannah, the Marketing Manager at Workspace Group. Hear firsthand how their team generates engaging descriptions for thousands of office units by integrating diverse data sources—from PDF floorplans to web pages—using FME transformers, like OpenAIVisionConnector and AnthropicVisionConnector. This use case will show you how GenAI can streamline content creation for marketing across the board.
Ollama Use Case: Learn how Scenario Specialist Dmitri Bagh has utilized Ollama within FME to input data, create custom models, and enhance security protocols. This segment will include demos to illustrate the full capabilities of FME in AI-driven processes.
Custom AI Models: Discover how to leverage FME to build personalized AI models using your data. Whether it’s populating a model with local data for added security or integrating public AI tools, find out how FME facilitates a versatile and secure approach to AI.
We’ll wrap up with a live Q&A session where you can engage with our experts on your specific use cases, and learn more about optimizing your data workflows with AI.
This webinar is ideal for professionals seeking to harness the power of AI within their data management systems while ensuring high levels of customization and security. Whether you're a novice or an expert, gain actionable insights and strategies to elevate your data processes. Join us to see how FME and AI can revolutionize how you work with data!
[OReilly Superstream] Occupy the Space: A grassroots guide to engineering (an...
The typical problem in product engineering is not bad strategy, so much as “no strategy”. This leads to confusion, lack of motivation, and incoherent action. The next time you look for a strategy and find an empty space, instead of waiting for it to be filled, I will show you how to fill it in yourself. If you’re wrong, it forces a correction. If you’re right, it helps create focus. I’ll share how I’ve approached this in the past, both what works and lessons for what didn’t work so well.
Principle of conventional tomography-Bibash Shahi ppt..pptx
before the computed tomography, it had been widely used.
JavaLand 2024: Application Development Green Masterplan
My presentation slides I used at JavaLand 2024
Monitoring and Managing Anomaly Detection on OpenShift.pdf
Monitoring and Managing Anomaly Detection on OpenShift
Overview
Dive into the world of anomaly detection on edge devices with our comprehensive hands-on tutorial. This SlideShare presentation will guide you through the entire process, from data collection and model training to edge deployment and real-time monitoring. Perfect for those looking to implement robust anomaly detection systems on resource-constrained IoT/edge devices.
Key Topics Covered
1. Introduction to Anomaly Detection
- Understand the fundamentals of anomaly detection and its importance in identifying unusual behavior or failures in systems.
2. Understanding Edge (IoT)
- Learn about edge computing and IoT, and how they enable real-time data processing and decision-making at the source.
3. What is ArgoCD?
- Discover ArgoCD, a declarative, GitOps continuous delivery tool for Kubernetes, and its role in deploying applications on edge devices.
4. Deployment Using ArgoCD for Edge Devices
- Step-by-step guide on deploying anomaly detection models on edge devices using ArgoCD.
5. Introduction to Apache Kafka and S3
- Explore Apache Kafka for real-time data streaming and Amazon S3 for scalable storage solutions.
6. Viewing Kafka Messages in the Data Lake
- Learn how to view and analyze Kafka messages stored in a data lake for better insights.
7. What is Prometheus?
- Get to know Prometheus, an open-source monitoring and alerting toolkit, and its application in monitoring edge devices.
8. Monitoring Application Metrics with Prometheus
- Detailed instructions on setting up Prometheus to monitor the performance and health of your anomaly detection system.
9. What is Camel K?
- Introduction to Camel K, a lightweight integration framework built on Apache Camel, designed for Kubernetes.
10. Configuring Camel K Integrations for Data Pipelines
- Learn how to configure Camel K for seamless data pipeline integrations in your anomaly detection workflow.
11. What is a Jupyter Notebook?
- Overview of Jupyter Notebooks, an open-source web application for creating and sharing documents with live code, equations, visualizations, and narrative text.
12. Jupyter Notebooks with Code Examples
- Hands-on examples and code snippets in Jupyter Notebooks to help you implement and test anomaly detection models.
Energy Efficient Video Encoding for Cloud and Edge Computing Instances
Energy Efficient Video Encoding for Cloud and Edge Computing Instances
Recently uploaded (20)
Nordic Marketo Engage User Group_June 13_ 2024.pptx
Nordic Marketo Engage User Group_June 13_ 2024.pptx
How to Interpret Trends in the Kalyan Rajdhani Mix Chart.pdf
How to Interpret Trends in the Kalyan Rajdhani Mix Chart.pdf
Introduction of Cybersecurity with OSS at Code Europe 2024
Introduction of Cybersecurity with OSS at Code Europe 2024
Programming Foundation Models with DSPy - Meetup Slides
Programming Foundation Models with DSPy - Meetup Slides
Your One-Stop Shop for Python Success: Top 10 US Python Development Providers
Your One-Stop Shop for Python Success: Top 10 US Python Development Providers
Dandelion Hashtable: beyond billion requests per second on a commodity server
Dandelion Hashtable: beyond billion requests per second on a commodity server
9 CEO's who hit $100m ARR Share Their Top Growth Tactics Nathan Latka, Founde...
9 CEO's who hit $100m ARR Share Their Top Growth Tactics Nathan Latka, Founde...
Choosing The Best AWS Service For Your Website + API.pptx
Choosing The Best AWS Service For Your Website + API.pptx
Driving Business Innovation: Latest Generative AI Advancements & Success Story
Driving Business Innovation: Latest Generative AI Advancements & Success Story
[OReilly Superstream] Occupy the Space: A grassroots guide to engineering (an...
[OReilly Superstream] Occupy the Space: A grassroots guide to engineering (an...
Principle of conventional tomography-Bibash Shahi ppt..pptx
Principle of conventional tomography-Bibash Shahi ppt..pptx
JavaLand 2024: Application Development Green Masterplan
JavaLand 2024: Application Development Green Masterplan
Monitoring and Managing Anomaly Detection on OpenShift.pdf
Monitoring and Managing Anomaly Detection on OpenShift.pdf
Energy Efficient Video Encoding for Cloud and Edge Computing Instances
Energy Efficient Video Encoding for Cloud and Edge Computing Instances
24 ch03proteins2008
- 3. AP Biology Proteins Most structurally & functionally diverse group Function: involved in almost everything enzymes (pepsin, DNA polymerase) structure (keratin, collagen) carriers & transport (hemoglobin, aquaporin) cell communication signals (insulin & other hormones) receptors defense (antibodies) movement (actin & myosin) storage (bean seed proteins)
- 4. AP Biology Proteins Structure monomer = amino acids 20 different amino acids polymer = polypeptide protein can be one or more polypeptide chains folded & bonded together large & complex molecules complex 3-D shape Rubisco hemoglobin growth hormones H2O
- 5. AP Biology Amino acids Structure central carbon amino group carboxyl group (acid) R group (side chain) variable group different for each amino acid confers unique chemical properties to each amino acid like 20 different letters of an alphabet can make many words (proteins) —N— H H C—OH || O R | —C— | H Oh, I get it! amino = NH2 acid = COOH
- 6. AP Biology Effect of different R groups: Nonpolar amino acids Why are these nonpolar & hydrophobic?Why are these nonpolar & hydrophobic? nonpolar & hydrophobic
- 7. AP Biology Effect of different R groups: Polar amino acids polar or charged & hydrophilic Why are these polar & hydrophillic?Why are these polar & hydrophillic?
- 8. AP Biology Ionizing in cellular waters H+ donorsH+ donors
- 9. AP Biology Ionizing in cellular waters H+ acceptorsH+ acceptors
- 10. AP Biology Sulfur containing amino acids Form disulfide bridges covalent cross links betweens sulfhydryls stabilizes 3-D structure You wondered why perms smell like rotten eggs? H-S – S-HH-S – S-H
- 11. AP Biology Building proteins Peptide bonds covalent bond between NH2 (amine) of one amino acid & COOH (carboxyl) of another C–N bond peptide bond dehydration synthesis H2O
- 12. AP Biology Building proteins Polypeptide chains have direction N-terminus = NH2 end C-terminus = COOH end repeated sequence (N-C-C) is the polypeptide backbone can only grow in one direction
- 13. AP Biology Protein structure & function hemoglobin Function depends on structure 3-D structure twisted, folded, coiled into unique shape collagen pepsin
- 14. AP Biology Primary (1°) structure Order of amino acids in chain amino acid sequence determined by gene (DNA) slight change in amino acid sequence can affect protein’s structure & its function even just one amino acid change can make all the difference! lysozyme: enzyme in tears & mucus that kills bacteria
- 15. AP Biology Sickle cell anemia I’m hydrophilic! But I’m hydrophobic! Just 1 out of 146 amino acids!
- 16. AP Biology Secondary (2°) structure “Local folding” folding along short sections of polypeptide interactions between adjacent amino acids H bonds weak bonds between R groups forms sections of 3-D structure α-helix β-pleated sheet
- 17. AP Biology Secondary (2°) structure
- 18. AP Biology Tertiary (3°) structure “Whole molecule folding” interactions between distant amino acids hydrophobic interactions cytoplasm is water-based nonpolar amino acids cluster away from water H bonds & ionic bonds disulfide bridges covalent bonds between sulfurs in sulfhydryls (S–H) anchors 3-D shape
- 19. AP Biology Quaternary (4°) structure More than one polypeptide chain bonded together only then does polypeptide become functional protein hydrophobic interactions collagen = skin & tendons hemoglobin
- 20. AP Biology Protein structure (review) amino acid sequence peptide bonds 1° determined by DNA R groups H bonds R groups hydrophobic interactions disulfide bridges (H & ionic bonds) 3° multiple polypeptides hydrophobic interactions 4° 2°
- 21. AP Biology Protein denaturation Unfolding a protein conditions that disrupt H bonds, ionic bonds, disulfide bridges temperature pH salinity alter 2° & 3° structure alter 3-D shape destroys functionality some proteins can return to their functional shape after denaturation, many cannot In Biology, size doesn’t matter, SHAPE matters!
- 22. 2008-2009AP Biology Let’s build some Proteins! EAT X
- 23. 2007-2008AP Biology Ghosts of Lectures Past (storage)
- 24. AP Biology Chaperonin proteins Guide protein folding provide shelter for folding polypeptides keep the new protein segregated from cytoplasmic influences
- 25. AP Biology Protein models Protein structure visualized by X-ray crystallography extrapolating from amino acid sequence computer modelling lysozyme
Editor's Notes
- clockwise: Rubisco — most important protein on the planet? Hemoglobin — a red blooded protein :-) Collagen — strings you together Growth Hormones — working hard in you right now!
- Storage: beans (seed proteins) Movement: muscle fibers Cell surface proteins: labels that ID cell as self vs. foreign Antibodies: recognize the labels ENZYMES!!!!
- Rubisco = 16 polypeptide chains Hemoglobin = 4 polypeptide chains (2 alpha, 2 beta)
- free COOH group on one end is ready to form another peptide bond so they “grow” in one direction from N-terminal to C-terminal
- Hemoglobin Hemoglobin is the protein that makes blood red. It is composed of four protein chains, two alpha chains and two beta chains, each with a ring-like heme group containing an iron atom. Oxygen binds reversibly to these iron atoms and is transported through blood. Pepsin Pepsin is the first in a series of enzymes in our digestive system that digest proteins. In the stomach, protein chains bind in the deep active site groove of pepsin, seen in the upper illustration (from PDB entry 5pep), and are broken into smaller pieces. Then, a variety of proteases and peptidases in the intestine finish the job. The small fragments--amino acids and dipeptides--are then absorbed by cells for use as metabolic fuel or construction of new proteins. Collagen– Your Most Plentiful Protein About one quarter of all of the protein in your body is collagen. Collagen is a major structural protein, forming molecular cables that strengthen the tendons and vast, resilient sheets that support the skin and internal organs. Bones and teeth are made by adding mineral crystals to collagen. Collagen provides structure to our bodies, protecting and supporting the softer tissues and connecting them with the skeleton. But, in spite of its critical function in the body, collagen is a relatively simple protein.
- Sickle cell anemia: 1 DNA letter changes 1 amino acid = serious disease Hemoglobin mutation: bends red blood cells out of shape & they clog your veins.
- glutamic acid is acidic & polar valine is non-polar = tries to “hide” from water of cell by sticking to another hemoglobin molecules.
- It’s a helix or B sheet within a single region. Can have both in one protein but a specific region is one or another
- How the whole thing holds together
- Structure equals function wonderfully illustrated by proteins Collagen is just like rope -- enables your skin to be strong and flexible.
- sequence determines structure and… structure determines function. Change the sequence & that changes the structure which changes the function.