Proteins
•Download as PPTX, PDF•
2 likes•122 views
Protein are the most abundant organic molecule of living systems. They occur in every part of the cell and constitutive about 50% of the cellular dry weight.Proteins form the fundamental basis of structure and functional unit of life. Unlike lipids and carbohydrates, proteins are not stored, so they must be consumed daily. Current recommended daily intake for adults is 0.8 grams of protein per kg of body weight (more is needed for children). Dietary protein comes from eating meat and milk.
Report
Share
Report
Share
Recommended
Biological roles of proteins
Proteins play very significant role in cell functioning. they are known as workhorse of cell. they are made up of amino acids.
Harish
This document discusses the structure and properties of proteins. It begins with an introduction stating that proteins are polymers of amino acids and are involved in most body functions. It then discusses the primary, secondary, tertiary, and quaternary levels of protein structure. The primary structure is the amino acid sequence. Secondary structures include alpha helices and beta pleated sheets formed by hydrogen bonds. Tertiary structure is determined by interactions between amino acid side chains. Quaternary structure results from multiple polypeptide subunits aggregating. Proteins have various properties like solubility, molecular weight, and shape. They also have important functions like structure, enzymes, hormones, and more.
Proteins Structure
Proteins are the most abundant organic molecules in living systems, making up about 50% of cellular dry weight. They occur throughout the cell and form the basic structure and functions of life. All proteins are polymers of amino acids. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids joined by peptide bonds. Secondary structure involves hydrogen bonding that causes regions of the polypeptide chain to fold into alpha helices or beta sheets. Tertiary structure describes the three-dimensional shape that proteins fold into. Quaternary structure refers to complexes of multiple polypeptide subunits.
Introduction to protein engg
This document provides an introduction to protein structure and function. It discusses that proteins are made up of amino acids and have different levels of structure, including primary, secondary, tertiary, and sometimes quaternary structure. The primary structure is the amino acid sequence. Secondary structure includes alpha helices and beta sheets formed by hydrogen bonds. Tertiary structure refers to the overall shape of the folded polypeptide chain. Quaternary structure describes the arrangement of multiple polypeptide subunits in a single protein. Understanding these hierarchical levels of structure is important for determining a protein's function.
Macromolecular structure and biological function of primary protiens
This document discusses primary proteins, their structure and functions. It begins with defining proteins as polymers of amino acids linked by peptide bonds. It then discusses the primary structure of proteins, which is the linear arrangement of amino acids. The key functions of proteins mentioned include acting as antibodies, enzymes, hormones, for transport, storage, as structural proteins, and contractile proteins. Some applications discussed are using proteins in coatings, food packaging, biotechnology, foods, microchips, and biomedical applications like hydrogels and targeted drug delivery.
Proteins and nucleic acids 2014
Proteins and nucleic acids are important macromolecules that make up cells. Proteins are composed of amino acids and perform critical functions like structure and catalysis. The four levels of protein structure are primary, secondary, tertiary, and quaternary. Nucleic acids DNA and RNA contain nitrogenous bases and sugars. DNA provides genetic instructions and replicates, while RNA has roles in protein synthesis. ATP is an energy-carrying molecule made from RNA nucleotides.
Structure And Function Of Macromolecules1
Macromolecules are polymers formed from monomers through dehydration or condensation reactions. Carbohydrates, proteins, lipids, and nucleic acids are major macromolecules. Carbohydrates include simple sugars and complex polysaccharides used for energy storage and structure. Proteins are polymers of amino acids with four levels of structure determining their function. Lipids are nonpolar and include fats, oils, and phospholipids that serve structural and energy roles. Nucleic acids like DNA are composed of nucleotides with phosphate, sugar and nitrogenous base components.
Apch5ppt
The document discusses the four main classes of macromolecules - carbohydrates, lipids, proteins, and nucleic acids. It describes their monomers, polymers, functions, and roles in energy storage, structure, and heredity. Carbohydrates include monosaccharides like glucose, disaccharides like sucrose, and polysaccharides like starch. Lipids are involved in long-term energy storage and consist of fatty acids and glycerol. Proteins have amino acids as monomers and perform control and structural functions. Nucleic acids like DNA and RNA are made of nucleotides and have roles in heredity, protein synthesis, and energy transfer.
Recommended
Biological roles of proteins
Proteins play very significant role in cell functioning. they are known as workhorse of cell. they are made up of amino acids.
Harish
This document discusses the structure and properties of proteins. It begins with an introduction stating that proteins are polymers of amino acids and are involved in most body functions. It then discusses the primary, secondary, tertiary, and quaternary levels of protein structure. The primary structure is the amino acid sequence. Secondary structures include alpha helices and beta pleated sheets formed by hydrogen bonds. Tertiary structure is determined by interactions between amino acid side chains. Quaternary structure results from multiple polypeptide subunits aggregating. Proteins have various properties like solubility, molecular weight, and shape. They also have important functions like structure, enzymes, hormones, and more.
Proteins Structure
Proteins are the most abundant organic molecules in living systems, making up about 50% of cellular dry weight. They occur throughout the cell and form the basic structure and functions of life. All proteins are polymers of amino acids. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids joined by peptide bonds. Secondary structure involves hydrogen bonding that causes regions of the polypeptide chain to fold into alpha helices or beta sheets. Tertiary structure describes the three-dimensional shape that proteins fold into. Quaternary structure refers to complexes of multiple polypeptide subunits.
Introduction to protein engg
This document provides an introduction to protein structure and function. It discusses that proteins are made up of amino acids and have different levels of structure, including primary, secondary, tertiary, and sometimes quaternary structure. The primary structure is the amino acid sequence. Secondary structure includes alpha helices and beta sheets formed by hydrogen bonds. Tertiary structure refers to the overall shape of the folded polypeptide chain. Quaternary structure describes the arrangement of multiple polypeptide subunits in a single protein. Understanding these hierarchical levels of structure is important for determining a protein's function.
Macromolecular structure and biological function of primary protiens
This document discusses primary proteins, their structure and functions. It begins with defining proteins as polymers of amino acids linked by peptide bonds. It then discusses the primary structure of proteins, which is the linear arrangement of amino acids. The key functions of proteins mentioned include acting as antibodies, enzymes, hormones, for transport, storage, as structural proteins, and contractile proteins. Some applications discussed are using proteins in coatings, food packaging, biotechnology, foods, microchips, and biomedical applications like hydrogels and targeted drug delivery.
Proteins and nucleic acids 2014
Proteins and nucleic acids are important macromolecules that make up cells. Proteins are composed of amino acids and perform critical functions like structure and catalysis. The four levels of protein structure are primary, secondary, tertiary, and quaternary. Nucleic acids DNA and RNA contain nitrogenous bases and sugars. DNA provides genetic instructions and replicates, while RNA has roles in protein synthesis. ATP is an energy-carrying molecule made from RNA nucleotides.
Structure And Function Of Macromolecules1
Macromolecules are polymers formed from monomers through dehydration or condensation reactions. Carbohydrates, proteins, lipids, and nucleic acids are major macromolecules. Carbohydrates include simple sugars and complex polysaccharides used for energy storage and structure. Proteins are polymers of amino acids with four levels of structure determining their function. Lipids are nonpolar and include fats, oils, and phospholipids that serve structural and energy roles. Nucleic acids like DNA are composed of nucleotides with phosphate, sugar and nitrogenous base components.
Apch5ppt
The document discusses the four main classes of macromolecules - carbohydrates, lipids, proteins, and nucleic acids. It describes their monomers, polymers, functions, and roles in energy storage, structure, and heredity. Carbohydrates include monosaccharides like glucose, disaccharides like sucrose, and polysaccharides like starch. Lipids are involved in long-term energy storage and consist of fatty acids and glycerol. Proteins have amino acids as monomers and perform control and structural functions. Nucleic acids like DNA and RNA are made of nucleotides and have roles in heredity, protein synthesis, and energy transfer.
Macromolecules
Carbon-based molecules are the foundation of life and come in three main structures: straight chains, branched chains, and rings. The four main types of carbon-based molecules found in living things are carbohydrates, lipids, proteins, and nucleic acids. Carbohydrates include monosaccharides like glucose and fructose that can link together to form polysaccharides like starch and cellulose. Lipids include fats, oils, and other nonpolar molecules that serve functions like energy storage. Proteins are polymers of amino acids that carry out important roles such as structure, movement, and catalysis. Nucleic acids like DNA and RNA are made of nucleotides and store and use genetic information.
Quaternary structure of protein
Quaternary structure refers to the arrangement of multiple protein subunits into a single protein complex. Hemoglobin is a common example that is made of two alpha and two beta subunits. The subunits interact through hydrophobic interactions, hydrogen bonding, and other bonds. Globular proteins tend to have quaternary structure that clusters the subunits into a spherical shape, while fibrous proteins form long coils or sheets through interactions between subunits. Quaternary structure allows proteins to take on specialized functions beyond what individual subunits could achieve alone.
The chemical_basis_for_life---organic_compounds
This document discusses the four major types of organic compounds found in living things: carbohydrates, lipids, proteins, and nucleic acids. It describes the structure and functions of each compound. Carbohydrates such as glucose provide energy, while lipids store energy and form cell membranes. Proteins have a variety of functions including maintaining cell shape and catalyzing reactions. Nucleic acids like DNA and RNA pass on traits by coding for amino acids and assembling proteins. Carbon is essential to life because it can form the large complex molecules that make up living organisms.
Biomolecules
Proteins are biologically important macromolecules composed of amino acid subunits linked by peptide bonds. There are two main types of protein structure - fibrous proteins have long parallel chains that form fibers while globular proteins coil into spherical shapes. Proteins are classified based on their composition, with simple proteins containing only amino acids while conjugated proteins also contain non-protein groups like carbohydrates. Protein structure is hierarchical, starting with the primary structure of the amino acid sequence, then secondary structures like alpha helices and beta sheets formed by hydrogen bonding, and finally the tertiary structure involving the protein's 3D conformation.
Biological molecules
Glycogen and cellulose are types of polysaccharides. Glycogen is the storage polysaccharide in animals, found mainly in muscle and liver, while cellulose is the main component of plant cell walls. DNA and RNA are nucleic acids that contain genetic information. DNA is made of nucleotides containing a phosphate group, deoxyribose sugar, and one of four nitrogenous bases. The order of bases in DNA contains the genetic code. Proteins are made of amino acids, which have an amino group, carboxyl group, hydrogen, and variable R group that gives each amino acid unique properties. Carbohydrates include monosaccharides like glucose, disaccharides made of two monosaccharides, and polysaccharides like
AS Level Biology - 1) Biological Molecules
To understand Biology, one must first understand the basic chemistry of it - which is relatively simple as opposed to normal chemistry. All you have to know about is Carbohydrate, Lipid, Protein and Water.
Chapter 3
This document discusses macromolecules and their structure and function. It focuses on proteins, carbohydrates, and lipids. Proteins are polymers of amino acids and their structure ranges from primary to quaternary levels. Carbohydrates include monosaccharides, disaccharides, and polysaccharides like starch and cellulose. Lipids are nonpolar and include triglycerides, fatty acids, and phospholipids that form cell membranes. The document explains the structure and properties of these macromolecules.
Organic Macromolecules
Organic macromolecules are giant molecules composed of many smaller subunits. The four main types of organic macromolecules are carbohydrates, lipids, proteins, and nucleic acids. Carbohydrates are used for energy storage and are made of monosaccharides like glucose. Lipids provide long-term energy storage and act as cushions, and are made of glycerol and fatty acids. Proteins perform most functions in the body as enzymes, hormones, and structures, and are composed of amino acids. Nucleic acids like DNA and RNA hold genetic information and are made of nucleotides.
Chemistry Of Cells
This document discusses the four main macromolecules found in cells: carbohydrates, lipids, nucleic acids, and proteins. Carbohydrates act as fuel for cells and are made of sugars. Lipids are mainly non-polar compounds that function in energy storage as triglycerides and in cell membranes as phospholipids. Nucleic acids like DNA and RNA store and transmit genetic information using nucleotides. Proteins have seven major functions and are made of amino acids arranged in unique sequences that determine 3D structure.
Proteins by anjali kotwal
Proteins are polymers of amino acids bonded by peptide linkages. They can be classified based on their chemical composition into simple proteins and conjugated proteins, or based on their molecular shape into fibrous proteins and globular proteins. Proteins have a complex structure that can be studied at four levels - primary, secondary, tertiary, and quaternary structure. Proteins are important biomolecules that serve essential functions in the body such as catalyzing biochemical reactions as enzymes and regulating metabolic processes as hormones.
structure, properties and biological functions of proteins.
The primary structure of a protein is its amino acid sequence. It has an N-terminal end with a free NH3+ group and a C-terminal end with a free COO- group. The secondary structure involves hydrogen bonding between amino acids and forms alpha helices, beta pleated sheets, or triple helices. The tertiary structure is the overall 3D shape from interactions between amino acid side chains far apart in the sequence. Quaternary structure refers to the association of multiple polypeptide chains in an oligomeric protein.
Macromolecules Lecture
The document summarizes the key macromolecules that make up living things: carbohydrates, lipids, proteins, and nucleic acids. It describes how each is made of monomers that polymerize through condensation reactions, and how their structures determine their functions. Carbohydrates include sugars and starches used for energy storage. Lipids include fats and phospholipids that store energy and make up cell membranes. Proteins have complex 4-level structures (primary to quaternary) that allow for their diverse functions like transport and muscle movement. Nucleic acids DNA and RNA contain nucleotides and code or aid in protein synthesis to pass on traits.
Architecture of proteins
Proteins are made up of amino acids joined together in chains that fold up into complex three-dimensional shapes determined by their primary, secondary, tertiary, and sometimes quaternary structure. There are 20 different amino acids that can be arranged in primary structures and then fold into secondary structures like alpha helices and beta sheets driven by hydrogen bonding. Tertiary structure describes how the whole chain folds into its final 3D shape through interactions between amino acid side chains. Some proteins have quaternary structure involving clustering of multiple chains.
Structure of protiens and the applied aspects
The slides explain the structures of proteins, the bond stabilizing the structure of amino acids, the different types of protein structures, the applied aspects and the newer advances in the protein structure.
2.4 & 7.3 Notes
Guided notes covering material from Topics 2.4 and 7.3 of the updated IB Biology syllabus for 2016 exams. Notes sequence and prompts are based on the Oxford IB Biology textbook by Allott and Mindorff.
Biological molecules
This document discusses biological molecules and biomolecules. It notes that the four most important elements that make up living things are carbon, hydrogen, oxygen, and nitrogen. Carbon is particularly important as it can form many different structures and molecules due to its ability to form up to four bonds. Biomolecules are organic molecules found in living organisms, including macromolecules like carbohydrates, proteins, lipids and nucleic acids. The document then discusses specific biomolecules like carbohydrates, lipids, proteins and water in more detail.
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.
Bio unit 1 biological elements and biomolecules notes
This document summarizes the key biological elements and biomolecules that make up all living things. It notes that all living things are made of atoms that bond together to form stable molecules. The six most important biological elements are carbon, hydrogen, oxygen, nitrogen, phosphorus, and sulfur. Carbon is particularly important as it can form four bonds, allowing it to create a diverse range of molecular structures and functions. The four main biomolecules are carbohydrates, lipids, proteins, and nucleic acids, each composed of various combinations of the six biological elements. These biomolecules serve essential roles like energy storage, structure, catalysis, and information transfer.
Biological macromolecules, M. Sc. Zoology, University of Mumbai.
The document discusses the key macromolecules that are essential for life - carbohydrates, proteins, lipids, and nucleic acids. It provides details on their monomers, polymers, functions, examples, and structural organization. The four macromolecules are large molecules formed by polymerization of smaller subunits. They perform critical roles like energy storage, structure, catalysis and information transfer in living organisms.
Lecture 4 molecules of life
The document discusses the four major classes of biological macromolecules - carbohydrates, lipids, proteins, and nucleic acids. It describes the monomers, polymers, and functions of each macromolecule class. It also discusses nutrition and interpreting food labels, noting health effects of obesity like diabetes and heart disease.
Proteins-Classification ,Structure of protein, properties and biological impo...
This document provides an overview of proteins, including their definition, classification, structure, and properties. It discusses how proteins are composed of amino acids and classified based on their chemical nature, structure, shape and solubility. The four levels of protein structure - primary, secondary, tertiary, and quaternary structure - are also summarized. Key properties of proteins like solubility, denaturation and functions in the body are highlighted. The document serves as an introduction to proteins and provides a high-level classification and structural overview.
Protein.pdf
Proteins have four levels of structure - primary, secondary, tertiary, and quaternary - which are stabilized by various forces. The primary structure is the linear sequence of amino acids joined by peptide bonds. Common secondary structures are alpha helices and beta sheets formed by hydrogen bonding. The tertiary structure is the final 3D shape determined by interactions between amino acid side chains. Quaternary structure involves interactions between multiple polypeptide subunits. Disruptions to protein structure can alter function, as seen when a single amino acid change in hemoglobin causes sickle cell disease.
More Related Content
What's hot
Macromolecules
Carbon-based molecules are the foundation of life and come in three main structures: straight chains, branched chains, and rings. The four main types of carbon-based molecules found in living things are carbohydrates, lipids, proteins, and nucleic acids. Carbohydrates include monosaccharides like glucose and fructose that can link together to form polysaccharides like starch and cellulose. Lipids include fats, oils, and other nonpolar molecules that serve functions like energy storage. Proteins are polymers of amino acids that carry out important roles such as structure, movement, and catalysis. Nucleic acids like DNA and RNA are made of nucleotides and store and use genetic information.
Quaternary structure of protein
Quaternary structure refers to the arrangement of multiple protein subunits into a single protein complex. Hemoglobin is a common example that is made of two alpha and two beta subunits. The subunits interact through hydrophobic interactions, hydrogen bonding, and other bonds. Globular proteins tend to have quaternary structure that clusters the subunits into a spherical shape, while fibrous proteins form long coils or sheets through interactions between subunits. Quaternary structure allows proteins to take on specialized functions beyond what individual subunits could achieve alone.
The chemical_basis_for_life---organic_compounds
This document discusses the four major types of organic compounds found in living things: carbohydrates, lipids, proteins, and nucleic acids. It describes the structure and functions of each compound. Carbohydrates such as glucose provide energy, while lipids store energy and form cell membranes. Proteins have a variety of functions including maintaining cell shape and catalyzing reactions. Nucleic acids like DNA and RNA pass on traits by coding for amino acids and assembling proteins. Carbon is essential to life because it can form the large complex molecules that make up living organisms.
Biomolecules
Proteins are biologically important macromolecules composed of amino acid subunits linked by peptide bonds. There are two main types of protein structure - fibrous proteins have long parallel chains that form fibers while globular proteins coil into spherical shapes. Proteins are classified based on their composition, with simple proteins containing only amino acids while conjugated proteins also contain non-protein groups like carbohydrates. Protein structure is hierarchical, starting with the primary structure of the amino acid sequence, then secondary structures like alpha helices and beta sheets formed by hydrogen bonding, and finally the tertiary structure involving the protein's 3D conformation.
Biological molecules
Glycogen and cellulose are types of polysaccharides. Glycogen is the storage polysaccharide in animals, found mainly in muscle and liver, while cellulose is the main component of plant cell walls. DNA and RNA are nucleic acids that contain genetic information. DNA is made of nucleotides containing a phosphate group, deoxyribose sugar, and one of four nitrogenous bases. The order of bases in DNA contains the genetic code. Proteins are made of amino acids, which have an amino group, carboxyl group, hydrogen, and variable R group that gives each amino acid unique properties. Carbohydrates include monosaccharides like glucose, disaccharides made of two monosaccharides, and polysaccharides like
AS Level Biology - 1) Biological Molecules
To understand Biology, one must first understand the basic chemistry of it - which is relatively simple as opposed to normal chemistry. All you have to know about is Carbohydrate, Lipid, Protein and Water.
Chapter 3
This document discusses macromolecules and their structure and function. It focuses on proteins, carbohydrates, and lipids. Proteins are polymers of amino acids and their structure ranges from primary to quaternary levels. Carbohydrates include monosaccharides, disaccharides, and polysaccharides like starch and cellulose. Lipids are nonpolar and include triglycerides, fatty acids, and phospholipids that form cell membranes. The document explains the structure and properties of these macromolecules.
Organic Macromolecules
Organic macromolecules are giant molecules composed of many smaller subunits. The four main types of organic macromolecules are carbohydrates, lipids, proteins, and nucleic acids. Carbohydrates are used for energy storage and are made of monosaccharides like glucose. Lipids provide long-term energy storage and act as cushions, and are made of glycerol and fatty acids. Proteins perform most functions in the body as enzymes, hormones, and structures, and are composed of amino acids. Nucleic acids like DNA and RNA hold genetic information and are made of nucleotides.
Chemistry Of Cells
This document discusses the four main macromolecules found in cells: carbohydrates, lipids, nucleic acids, and proteins. Carbohydrates act as fuel for cells and are made of sugars. Lipids are mainly non-polar compounds that function in energy storage as triglycerides and in cell membranes as phospholipids. Nucleic acids like DNA and RNA store and transmit genetic information using nucleotides. Proteins have seven major functions and are made of amino acids arranged in unique sequences that determine 3D structure.
Proteins by anjali kotwal
Proteins are polymers of amino acids bonded by peptide linkages. They can be classified based on their chemical composition into simple proteins and conjugated proteins, or based on their molecular shape into fibrous proteins and globular proteins. Proteins have a complex structure that can be studied at four levels - primary, secondary, tertiary, and quaternary structure. Proteins are important biomolecules that serve essential functions in the body such as catalyzing biochemical reactions as enzymes and regulating metabolic processes as hormones.
structure, properties and biological functions of proteins.
The primary structure of a protein is its amino acid sequence. It has an N-terminal end with a free NH3+ group and a C-terminal end with a free COO- group. The secondary structure involves hydrogen bonding between amino acids and forms alpha helices, beta pleated sheets, or triple helices. The tertiary structure is the overall 3D shape from interactions between amino acid side chains far apart in the sequence. Quaternary structure refers to the association of multiple polypeptide chains in an oligomeric protein.
Macromolecules Lecture
The document summarizes the key macromolecules that make up living things: carbohydrates, lipids, proteins, and nucleic acids. It describes how each is made of monomers that polymerize through condensation reactions, and how their structures determine their functions. Carbohydrates include sugars and starches used for energy storage. Lipids include fats and phospholipids that store energy and make up cell membranes. Proteins have complex 4-level structures (primary to quaternary) that allow for their diverse functions like transport and muscle movement. Nucleic acids DNA and RNA contain nucleotides and code or aid in protein synthesis to pass on traits.
Architecture of proteins
Proteins are made up of amino acids joined together in chains that fold up into complex three-dimensional shapes determined by their primary, secondary, tertiary, and sometimes quaternary structure. There are 20 different amino acids that can be arranged in primary structures and then fold into secondary structures like alpha helices and beta sheets driven by hydrogen bonding. Tertiary structure describes how the whole chain folds into its final 3D shape through interactions between amino acid side chains. Some proteins have quaternary structure involving clustering of multiple chains.
Structure of protiens and the applied aspects
The slides explain the structures of proteins, the bond stabilizing the structure of amino acids, the different types of protein structures, the applied aspects and the newer advances in the protein structure.
2.4 & 7.3 Notes
Guided notes covering material from Topics 2.4 and 7.3 of the updated IB Biology syllabus for 2016 exams. Notes sequence and prompts are based on the Oxford IB Biology textbook by Allott and Mindorff.
Biological molecules
This document discusses biological molecules and biomolecules. It notes that the four most important elements that make up living things are carbon, hydrogen, oxygen, and nitrogen. Carbon is particularly important as it can form many different structures and molecules due to its ability to form up to four bonds. Biomolecules are organic molecules found in living organisms, including macromolecules like carbohydrates, proteins, lipids and nucleic acids. The document then discusses specific biomolecules like carbohydrates, lipids, proteins and water in more detail.
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.
Bio unit 1 biological elements and biomolecules notes
This document summarizes the key biological elements and biomolecules that make up all living things. It notes that all living things are made of atoms that bond together to form stable molecules. The six most important biological elements are carbon, hydrogen, oxygen, nitrogen, phosphorus, and sulfur. Carbon is particularly important as it can form four bonds, allowing it to create a diverse range of molecular structures and functions. The four main biomolecules are carbohydrates, lipids, proteins, and nucleic acids, each composed of various combinations of the six biological elements. These biomolecules serve essential roles like energy storage, structure, catalysis, and information transfer.
Biological macromolecules, M. Sc. Zoology, University of Mumbai.
The document discusses the key macromolecules that are essential for life - carbohydrates, proteins, lipids, and nucleic acids. It provides details on their monomers, polymers, functions, examples, and structural organization. The four macromolecules are large molecules formed by polymerization of smaller subunits. They perform critical roles like energy storage, structure, catalysis and information transfer in living organisms.
Lecture 4 molecules of life
The document discusses the four major classes of biological macromolecules - carbohydrates, lipids, proteins, and nucleic acids. It describes the monomers, polymers, and functions of each macromolecule class. It also discusses nutrition and interpreting food labels, noting health effects of obesity like diabetes and heart disease.
What's hot (20)
structure, properties and biological functions of proteins.
structure, properties and biological functions of proteins.
Bio unit 1 biological elements and biomolecules notes
Bio unit 1 biological elements and biomolecules notes
Biological macromolecules, M. Sc. Zoology, University of Mumbai.
Biological macromolecules, M. Sc. Zoology, University of Mumbai.
Similar to Proteins
Proteins-Classification ,Structure of protein, properties and biological impo...
This document provides an overview of proteins, including their definition, classification, structure, and properties. It discusses how proteins are composed of amino acids and classified based on their chemical nature, structure, shape and solubility. The four levels of protein structure - primary, secondary, tertiary, and quaternary structure - are also summarized. Key properties of proteins like solubility, denaturation and functions in the body are highlighted. The document serves as an introduction to proteins and provides a high-level classification and structural overview.
Protein.pdf
Proteins have four levels of structure - primary, secondary, tertiary, and quaternary - which are stabilized by various forces. The primary structure is the linear sequence of amino acids joined by peptide bonds. Common secondary structures are alpha helices and beta sheets formed by hydrogen bonding. The tertiary structure is the final 3D shape determined by interactions between amino acid side chains. Quaternary structure involves interactions between multiple polypeptide subunits. Disruptions to protein structure can alter function, as seen when a single amino acid change in hemoglobin causes sickle cell disease.
Introduction to Proteins and Aminoacids with Clinical significance
This document discusses proteins, including their structure and properties. It provides definitions of key protein terms like amino acids, peptides, and the four levels of protein structure - primary, secondary, tertiary, and quaternary. It also summarizes factors that can cause protein denaturation, like heat, acids, bases, and alcohol, disrupting the shapes and bonds of protein molecules. Food sources of protein from both animal and plant sources are listed.
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.
Proteins
Proteins are essential macromolecules that make up 20% of the human body. They are composed of amino acids and perform many critical functions including structure, regulation, catalysis, movement and more. Protein synthesis occurs in ribosomes within cells. Proteins are not stored but are broken down if excess amino acids are consumed. They have primary, secondary, tertiary and quaternary levels of structure determined by amino acid sequence and interactions. There are 20 standard amino acids that are linked by peptide bonds to form proteins.
module 7.pptx
Macromolecules are very large molecules formed by polymerization of smaller monomers. Macromolecules contain more than 10,000 atoms. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the simple sequence of amino acids in the protein chain. The secondary structure depends on local interactions between parts of the chain and can form alpha helices or beta pleated sheets. Tertiary structure refers to the overall 3D shape after secondary interactions. Quaternary structure involves multiple polypeptide chains linked together, such as the four chains in hemoglobin.
Protein and it's structure and functions
The document discusses the structure and biological significance of proteins. It describes the 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 bonding that forms alpha helices or beta sheets. Tertiary structure defines the overall 3D shape formed by interactions between amino acid side chains. Quaternary structure refers to the clustering of multiple peptide chains through various bonds. Proteins are essential to life and constitute 50% of cellular material.
Protein structure
Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structures include alpha helices and beta sheets formed by hydrogen bonding of the polypeptide chain. Tertiary structure refers to the overall three-dimensional shape that results from interactions between amino acid side chains. Quaternary structure involves interactions between multiple protein subunits.
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
Proteins.pdf
Proteins are polypeptide structures made up of one or more extended chains of residues from the amino acid. They provide a wide range of organism tasks, including as DNA replication, molecule transport, metabolic process catalysis, and cell structural support.
The albumins seen in vast quantities in egg whites typically have a distinct 3D structure as a result of bonds that form between the protein’s various amino acids. These bonds are broken by heating, exposing the hydrophobic (water-hating) amino acids that are typically maintained on the inside of the protein 1, 1 comma, 2 end superscript, 2, start superscript. In an effort to escape the water that surrounds them in the egg white, the hydrophobic amino acids will bind to one another, creating a protein network that gives the egg white structure and makes it white and opaque. Ta-da! Protein denaturation, thank you for another wonderful breakfast
Amino Acids and Protein
Study Material for B.Sc. Students
Primary, secondary, tertiary, quaternary structures of protein, motiffs and domains, subunits
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.
Lecture 5 bio
This document discusses the structure and function of macromolecules. It focuses on proteins, which are polymers of amino acids that fold into complex shapes to perform various functions in the body. The four levels of protein structure are described as primary, secondary, tertiary, and quaternary. Lipids are also covered, with details about their hydrophobic nature and roles as fats, phospholipids in cell membranes, and steroids like cholesterol.
Protein & amino acid (ulivina pratini)
This document discusses amino acids and proteins. It begins by defining proteins as polymers of amino acids and describing the basic structure of amino acids. It then covers the different configurations of amino acids, their properties in aqueous solutions, and classifications. The document also discusses the structures of peptides and proteins at the primary, secondary, tertiary, and quaternary levels. It describes the digestion and metabolism of amino acids as well as the urea cycle. Finally, it provides an overview of protein biosynthesis, including the roles of DNA, mRNA, tRNA, and ribosomes.
Protein structures by amina
Proteins have four levels of structure:
1) Primary structure is the linear sequence of amino acids in the polypeptide chain held together by peptide bonds.
2) Secondary structure involves the local 3D structure of portions of the chain, forming alpha helices or beta sheets.
3) Tertiary structure describes the overall 3D structure of a single polypeptide chain, including side chains.
4) Quaternary structure refers to the 3D arrangement of multiple polypeptide subunits that make up a single protein.
Protein structure
- Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids in the polypeptide chain. Secondary structure involves hydrogen bonding that forms alpha helices and beta sheets. Tertiary structure is the 3D shape formed by interactions between different parts of the polypeptide. Quaternary structure refers to the assembly of multiple polypeptide subunits.
Proteins & amino acids (ulivina pratini)
This document discusses amino acids and proteins. It begins by defining proteins as being formed from amino acids, which are the monomers or building blocks of proteins. The document then covers the structure of amino acids, including their general formula and configurations. It also discusses the properties of amino acids in aqueous solutions and their classification as essential or non-essential. The document goes on to explain how amino acids can bond together to form peptides and polypeptides, and the levels of protein structure from primary to quaternary. It concludes with sections on the metabolism of proteins and amino acids in the body.
Structure and function of protein
This document is a presentation on molecular biology given by Mujeeb Ur Rehman to Dr. Abid Jan. It discusses the key topics of proteins, amino acids, and protein structure. Specifically, it covers the 20 standard amino acids, how they are classified, and how they come together to form the primary, secondary, tertiary, and quaternary structures of proteins through covalent and non-covalent bonds. Forces like hydrogen bonds, ionic bonds, and hydrophobic interactions contribute to stable protein folding and structure formation at each level.
Similar to Proteins (20)
Proteins-Classification ,Structure of protein, properties and biological impo...
Proteins-Classification ,Structure of protein, properties and biological impo...
Introduction to Proteins and Aminoacids with Clinical significance
Introduction to Proteins and Aminoacids with Clinical significance
Proteins_Energy_____________Metabolism___importance.pdf
Proteins_Energy_____________Metabolism___importance.pdf
Proteins_Energy_____________Metabolism___importance.pdf
Proteins_Energy_____________Metabolism___importance.pdf
Protein metabolism and nitrogen fixation and metabolism
Protein metabolism and nitrogen fixation and metabolism
More from Shri Shankaracharya College, Bhilai,Junwani
Environment Economics &Ethics invisible hand & Malthusian theory
Environment Economics &Ethics invisible hand & Malthusian theoryShri Shankaracharya College, Bhilai,Junwani
The document discusses the relationship between economics, environment, and ethics. It summarizes that we are facing issues today because of ignoring the fundamental relationship between the three. The economy relies on ecosystem services provided by the environment, but the environment is being degraded by waste and emissions. Ethical practices also constitute an unseen force guiding economic behavior.Azadi ka amrut mahotsav, Mahilayon ka yogdan swatantrata Sangram mein
Azadi ka amrut mahotsav, Mahilayon ka yogdan swatantrata Sangram meinShri Shankaracharya College, Bhilai,Junwani
The document discusses the benefits of exercise for mental health. Regular physical activity can help reduce anxiety and depression and improve mood and cognitive function. Exercise causes chemical changes in the brain that may help protect against mental illness and improve symptoms for those who already suffer from conditions like anxiety and depression.B.ed 1,scientific temper
Scientific temper and attitude refer to traits like critical thinking, objectivity, open-mindedness, and respect for evidence. Developing a scientific attitude in students is the aim of science teaching. Some key aspects of scientific attitude are questioning beliefs, reasoning logically, honestly reporting observations, and accepting ideas that are supported by evidence. Fostering skills like curiosity, perseverance, and skepticism in students can help cultivate their scientific temper.
Aims and objectives of bio. sci. 14 9-20
This document discusses the aims and objectives of teaching biological science. It begins by defining biological science as the study of life and living organisms. It then lists several objectives of teaching biological science, including developing students' scientific outlook, curiosity about their surroundings, and respect for nature. The document also discusses the values of teaching biological science, which include encouraging curiosity and knowledge, and keeping an open mind. It emphasizes that teaching biological science should help students become responsible democratic citizens and appreciate diverse perspectives. Overall, the document provides an overview of the goals and importance of teaching biological science.
Ict application in bio.sc.24 9
This presentation discusses using information and communication technologies (ICT) applications in biology learning. It introduces the topic, noting the presenter and institution. The document provides references on the advantages and limitations of ICT in education, using ICT to integrate science teaching and learning, and the impact of ICT in education.
Runges kutta method
B.Sc. III mathematics numerical analysis paper - III
Shri shankaracharya Mahavidyalaya junwani bhilai.
Isolation & preservation of culture of microorganism
The term isolation refers to the separation of a strain from a natural, mixed population of living microbes, as present in the environment. It becomes necessary to maintain the viability and purity of the microorganism by keeping the pure culture free from contamination.
Basics concept of physical chemistry
1) The document discusses oxidation-reduction (redox) reactions and concepts related to solution concentrations. It defines oxidizing and reducing agents and gives examples of each.
2) A redox reaction involves the simultaneous oxidation and reduction of reactants. In redox reactions, the total increase in oxidation number equals the total decrease.
3) Disproportionation reactions involve the same element in a compound being both oxidized and reduced. The reverse is called a comproportionation reaction.
indifference curve
The document discusses the benefits of exercise for mental health. Regular physical activity can help reduce anxiety and depression and improve mood and cognitive functioning. Exercise boosts blood flow, releases endorphins, and promotes changes in the brain which help enhance one's emotional well-being and mental clarity.
Equilibrium
The document discusses the concept of equilibrium in economics. It defines equilibrium as a state of balance where opposing forces neutralize each other. In microeconomics, market equilibrium occurs when supply equals demand. In macroeconomics, equilibrium is reached when aggregate demand equals aggregate supply. The document provides examples of economic disequilibrium and equilibrium, and examines how prices adjust via demand and supply mechanisms to reach equilibrium. Key terms in Hindi are also defined.
Crystal field theory
This document summarizes Crystal Field Theory, which considers the electrostatic interactions between metal ions and ligands. It describes ligands and metal ions as point charges that can have attractive or repulsive forces. This causes the d orbitals of the metal ion to split into two sets depending on if the field created by the ligands is weak or strong. The theory explains color in coordination compounds as being caused by d-d electron transitions under the influence of ligands. However, it has limitations like not accounting for other metal orbitals or the partial covalent nature of metal-ligand bonds.
Utility
Dr. Laxmi Verma teaches Microeconomics at the BA-1 level and her topic is on utility in Unit 1 of the course. She teaches at Shri Shankracharya Mahavidyalya in Junwani.
New economic reform
Dr. Laxmi Verma is teaching a class of B.A-1 students. The subject is Indian Economy and the topic being covered is New Economic Reform. The document provides basic context about an economics lecture being given to undergraduate students on recent reforms in the Indian economy.
Iso product Curve
An iso-product curve shows the different combinations of two factors of production, such as labor and capital, that result in the same level of output. It is represented graphically, with the two factors on the x and y axes and points of equal output connected to form an iso-product curve. Key properties are that iso-product curves slope downward to the right, are convex to the origin, and do not intersect, as each curve represents a different output level. Higher iso-product curves correspond to higher output levels. Iso-product curves allow producers to identify input combinations that achieve maximum output efficiently.
Demand theory
This document discusses demand theory and the relationship between supply and demand. It covers the following key points:
1) Demand theory explains how consumer demand for goods and services relates to their prices in the market. It forms the basis for the demand curve, which shows that as price increases, demand decreases.
2) Demand depends on the utility of goods in satisfying wants and needs as well as a consumer's ability to pay. Supply and demand determine market prices and reach equilibrium when supply equals demand.
3) The demand curve has a negative slope, showing an inverse relationship between price and quantity demanded. A change in non-price factors like income can shift the demand curve. The law of supply and
Land reform
Land reform in India has involved abolishing intermediaries like rent collectors and establishing ceilings on land ownership to redistribute surplus land to the landless. The goals were to remove impediments to agricultural production from the previous feudal system and eliminate exploitation. Key reforms included abolishing rent collectors, regulating tenancy, imposing landholding ceilings, consolidating fragmented holdings, and promoting cooperative farming. Impacts included reducing disparities, giving ex-landlords other work, increasing revenue, and empowering small farmers and laborers. Land reform aimed to promote social justice and economic growth through a more equitable distribution of agricultural land.
Isomerism
This document discusses different types of structural isomerism that can occur in coordination compounds. It defines structural isomerism as compounds having the same molecular formula but different physical and chemical properties due to different structures or orientations. The types of structural isomerism discussed include ionization isomerism, solvate/hydrate isomerism, linkage isomerism, coordination isomerism, ligand isomerism, polymerization isomerism, geometrical isomerism (cis/trans), and optical isomerism. Examples are provided to illustrate each type of isomerism.
More from Shri Shankaracharya College, Bhilai,Junwani (20)
Environment Economics &Ethics invisible hand & Malthusian theory
Environment Economics &Ethics invisible hand & Malthusian theory
Azadi ka amrut mahotsav, Mahilayon ka yogdan swatantrata Sangram mein
Azadi ka amrut mahotsav, Mahilayon ka yogdan swatantrata Sangram mein
Isolation & preservation of culture of microorganism
Isolation & preservation of culture of microorganism
Recently uploaded
Authoring a personal GPT for your research and practice: How we created the Q...
Thematic analysis in qualitative research is a time-consuming and systematic task, typically done using teams. Team members must ground their activities on common understandings of the major concepts underlying the thematic analysis, and define criteria for its development. However, conceptual misunderstandings, equivocations, and lack of adherence to criteria are challenges to the quality and speed of this process. Given the distributed and uncertain nature of this process, we wondered if the tasks in thematic analysis could be supported by readily available artificial intelligence chatbots. Our early efforts point to potential benefits: not just saving time in the coding process but better adherence to criteria and grounding, by increasing triangulation between humans and artificial intelligence. This tutorial will provide a description and demonstration of the process we followed, as two academic researchers, to develop a custom ChatGPT to assist with qualitative coding in the thematic data analysis process of immersive learning accounts in a survey of the academic literature: QUAL-E Immersive Learning Thematic Analysis Helper. In the hands-on time, participants will try out QUAL-E and develop their ideas for their own qualitative coding ChatGPT. Participants that have the paid ChatGPT Plus subscription can create a draft of their assistants. The organizers will provide course materials and slide deck that participants will be able to utilize to continue development of their custom GPT. The paid subscription to ChatGPT Plus is not required to participate in this workshop, just for trying out personal GPTs during it.
Phenomics assisted breeding in crop improvement
As the population is increasing and will reach about 9 billion upto 2050. Also due to climate change, it is difficult to meet the food requirement of such a large population. Facing the challenges presented by resource shortages, climate
change, and increasing global population, crop yield and quality need to be improved in a sustainable way over the coming decades. Genetic improvement by breeding is the best way to increase crop productivity. With the rapid progression of functional
genomics, an increasing number of crop genomes have been sequenced and dozens of genes influencing key agronomic traits have been identified. However, current genome sequence information has not been adequately exploited for understanding
the complex characteristics of multiple gene, owing to a lack of crop phenotypic data. Efficient, automatic, and accurate technologies and platforms that can capture phenotypic data that can
be linked to genomics information for crop improvement at all growth stages have become as important as genotyping. Thus,
high-throughput phenotyping has become the major bottleneck restricting crop breeding. Plant phenomics has been defined as the high-throughput, accurate acquisition and analysis of multi-dimensional phenotypes
during crop growing stages at the organism level, including the cell, tissue, organ, individual plant, plot, and field levels. With the rapid development of novel sensors, imaging technology,
and analysis methods, numerous infrastructure platforms have been developed for phenotyping.
Sharlene Leurig - Enabling Onsite Water Use with Net Zero Water
Sharlene Leurig - Enabling Onsite Water Use with Net Zero WaterTexas Alliance of Groundwater Districts
Presented at June 6-7 Texas Alliance of Groundwater Districts Business MeetingEWOCS-I: The catalog of X-ray sources in Westerlund 1 from the Extended Weste...
Context. With a mass exceeding several 104 M⊙ and a rich and dense population of massive stars, supermassive young star clusters
represent the most massive star-forming environment that is dominated by the feedback from massive stars and gravitational interactions
among stars.
Aims. In this paper we present the Extended Westerlund 1 and 2 Open Clusters Survey (EWOCS) project, which aims to investigate
the influence of the starburst environment on the formation of stars and planets, and on the evolution of both low and high mass stars.
The primary targets of this project are Westerlund 1 and 2, the closest supermassive star clusters to the Sun.
Methods. The project is based primarily on recent observations conducted with the Chandra and JWST observatories. Specifically,
the Chandra survey of Westerlund 1 consists of 36 new ACIS-I observations, nearly co-pointed, for a total exposure time of 1 Msec.
Additionally, we included 8 archival Chandra/ACIS-S observations. This paper presents the resulting catalog of X-ray sources within
and around Westerlund 1. Sources were detected by combining various existing methods, and photon extraction and source validation
were carried out using the ACIS-Extract software.
Results. The EWOCS X-ray catalog comprises 5963 validated sources out of the 9420 initially provided to ACIS-Extract, reaching a
photon flux threshold of approximately 2 × 10−8 photons cm−2
s
−1
. The X-ray sources exhibit a highly concentrated spatial distribution,
with 1075 sources located within the central 1 arcmin. We have successfully detected X-ray emissions from 126 out of the 166 known
massive stars of the cluster, and we have collected over 71 000 photons from the magnetar CXO J164710.20-455217.
Equivariant neural networks and representation theory
Or: Beyond linear.
Abstract: Equivariant neural networks are neural networks that incorporate symmetries. The nonlinear activation functions in these networks result in interesting nonlinear equivariant maps between simple representations, and motivate the key player of this talk: piecewise linear representation theory.
Disclaimer: No one is perfect, so please mind that there might be mistakes and typos.
dtubbenhauer@gmail.com
Corrected slides: dtubbenhauer.com/talks.html
The use of Nauplii and metanauplii artemia in aquaculture (brine shrimp).pptx
Although Artemia has been known to man for centuries, its use as a food for the culture of larval organisms apparently began only in the 1930s, when several investigators found that it made an excellent food for newly hatched fish larvae (Litvinenko et al., 2023). As aquaculture developed in the 1960s and ‘70s, the use of Artemia also became more widespread, due both to its convenience and to its nutritional value for larval organisms (Arenas-Pardo et al., 2024). The fact that Artemia dormant cysts can be stored for long periods in cans, and then used as an off-the-shelf food requiring only 24 h of incubation makes them the most convenient, least labor-intensive, live food available for aquaculture (Sorgeloos & Roubach, 2021). The nutritional value of Artemia, especially for marine organisms, is not constant, but varies both geographically and temporally. During the last decade, however, both the causes of Artemia nutritional variability and methods to improve poorquality Artemia have been identified (Loufi et al., 2024).
Brine shrimp (Artemia spp.) are used in marine aquaculture worldwide. Annually, more than 2,000 metric tons of dry cysts are used for cultivation of fish, crustacean, and shellfish larva. Brine shrimp are important to aquaculture because newly hatched brine shrimp nauplii (larvae) provide a food source for many fish fry (Mozanzadeh et al., 2021). Culture and harvesting of brine shrimp eggs represents another aspect of the aquaculture industry. Nauplii and metanauplii of Artemia, commonly known as brine shrimp, play a crucial role in aquaculture due to their nutritional value and suitability as live feed for many aquatic species, particularly in larval stages (Sorgeloos & Roubach, 2021).
20240520 Planning a Circuit Simulator in JavaScript.pptx
Evaporation step counter work. I have done a physical experiment.
(Work in progress.)
Unlocking the mysteries of reproduction: Exploring fecundity and gonadosomati...
The pygmy halfbeak Dermogenys colletei, is known for its viviparous nature, this presents an intriguing case of relatively low fecundity, raising questions about potential compensatory reproductive strategies employed by this species. Our study delves into the examination of fecundity and the Gonadosomatic Index (GSI) in the Pygmy Halfbeak, D. colletei (Meisner, 2001), an intriguing viviparous fish indigenous to Sarawak, Borneo. We hypothesize that the Pygmy halfbeak, D. colletei, may exhibit unique reproductive adaptations to offset its low fecundity, thus enhancing its survival and fitness. To address this, we conducted a comprehensive study utilizing 28 mature female specimens of D. colletei, carefully measuring fecundity and GSI to shed light on the reproductive adaptations of this species. Our findings reveal that D. colletei indeed exhibits low fecundity, with a mean of 16.76 ± 2.01, and a mean GSI of 12.83 ± 1.27, providing crucial insights into the reproductive mechanisms at play in this species. These results underscore the existence of unique reproductive strategies in D. colletei, enabling its adaptation and persistence in Borneo's diverse aquatic ecosystems, and call for further ecological research to elucidate these mechanisms. This study lends to a better understanding of viviparous fish in Borneo and contributes to the broader field of aquatic ecology, enhancing our knowledge of species adaptations to unique ecological challenges.
Bob Reedy - Nitrate in Texas Groundwater.pdf
Presented at June 6-7 Texas Alliance of Groundwater Districts Business Meeting
The cost of acquiring information by natural selection
This is a short talk that I gave at the Banff International Research Station workshop on Modeling and Theory in Population Biology. The idea is to try to understand how the burden of natural selection relates to the amount of information that selection puts into the genome.
It's based on the first part of this research paper:
The cost of information acquisition by natural selection
Ryan Seamus McGee, Olivia Kosterlitz, Artem Kaznatcheev, Benjamin Kerr, Carl T. Bergstrom
bioRxiv 2022.07.02.498577; doi: https://doi.org/10.1101/2022.07.02.498577
The debris of the ‘last major merger’ is dynamically young
The Milky Way’s (MW) inner stellar halo contains an [Fe/H]-rich component with highly eccentric orbits, often referred to as the
‘last major merger.’ Hypotheses for the origin of this component include Gaia-Sausage/Enceladus (GSE), where the progenitor
collided with the MW proto-disc 8–11 Gyr ago, and the Virgo Radial Merger (VRM), where the progenitor collided with the
MW disc within the last 3 Gyr. These two scenarios make different predictions about observable structure in local phase space,
because the morphology of debris depends on how long it has had to phase mix. The recently identified phase-space folds in Gaia
DR3 have positive caustic velocities, making them fundamentally different than the phase-mixed chevrons found in simulations
at late times. Roughly 20 per cent of the stars in the prograde local stellar halo are associated with the observed caustics. Based
on a simple phase-mixing model, the observed number of caustics are consistent with a merger that occurred 1–2 Gyr ago.
We also compare the observed phase-space distribution to FIRE-2 Latte simulations of GSE-like mergers, using a quantitative
measurement of phase mixing (2D causticality). The observed local phase-space distribution best matches the simulated data
1–2 Gyr after collision, and certainly not later than 3 Gyr. This is further evidence that the progenitor of the ‘last major merger’
did not collide with the MW proto-disc at early times, as is thought for the GSE, but instead collided with the MW disc within
the last few Gyr, consistent with the body of work surrounding the VRM.
The binding of cosmological structures by massless topological defects
Assuming spherical symmetry and weak field, it is shown that if one solves the Poisson equation or the Einstein field
equations sourced by a topological defect, i.e. a singularity of a very specific form, the result is a localized gravitational
field capable of driving flat rotation (i.e. Keplerian circular orbits at a constant speed for all radii) of test masses on a thin
spherical shell without any underlying mass. Moreover, a large-scale structure which exploits this solution by assembling
concentrically a number of such topological defects can establish a flat stellar or galactic rotation curve, and can also deflect
light in the same manner as an equipotential (isothermal) sphere. Thus, the need for dark matter or modified gravity theory is
mitigated, at least in part.
THEMATIC APPERCEPTION TEST(TAT) cognitive abilities, creativity, and critic...
THEMATIC APPERCEPTION TEST(TAT) cognitive abilities, creativity, and critic...Abdul Wali Khan University Mardan,kP,Pakistan
hematic appreciation test is a psychological assessment tool used to measure an individual's appreciation and understanding of specific themes or topics. This test helps to evaluate an individual's ability to connect different ideas and concepts within a given theme, as well as their overall comprehension and interpretation skills. The results of the test can provide valuable insights into an individual's cognitive abilities, creativity, and critical thinking skillsESA/ACT Science Coffee: Diego Blas - Gravitational wave detection with orbita...
ESA/ACT Science Coffee: Diego Blas - Gravitational wave detection with orbita...Advanced-Concepts-Team
Presentation in the Science Coffee of the Advanced Concepts Team of the European Space Agency on the 07.06.2024.
Speaker: Diego Blas (IFAE/ICREA)
Title: Gravitational wave detection with orbital motion of Moon and artificial
Abstract:
In this talk I will describe some recent ideas to find gravitational waves from supermassive black holes or of primordial origin by studying their secular effect on the orbital motion of the Moon or satellites that are laser ranged.Remote Sensing and Computational, Evolutionary, Supercomputing, and Intellige...
Remote Sensing and Computational, Evolutionary, Supercomputing, and Intellige...University of Maribor
Slides from talk:
Aleš Zamuda: Remote Sensing and Computational, Evolutionary, Supercomputing, and Intelligent Systems.
11th International Conference on Electrical, Electronics and Computer Engineering (IcETRAN), Niš, 3-6 June 2024
Inter-Society Networking Panel GRSS/MTT-S/CIS Panel Session: Promoting Connection and Cooperation
https://www.etran.rs/2024/en/home-english/8.Isolation of pure cultures and preservation of cultures.pdf
Isolation of pure culture, its various method.
Describing and Interpreting an Immersive Learning Case with the Immersion Cub...
Current descriptions of immersive learning cases are often difficult or impossible to compare. This is due to a myriad of different options on what details to include, which aspects are relevant, and on the descriptive approaches employed. Also, these aspects often combine very specific details with more general guidelines or indicate intents and rationales without clarifying their implementation. In this paper we provide a method to describe immersive learning cases that is structured to enable comparisons, yet flexible enough to allow researchers and practitioners to decide which aspects to include. This method leverages a taxonomy that classifies educational aspects at three levels (uses, practices, and strategies) and then utilizes two frameworks, the Immersive Learning Brain and the Immersion Cube, to enable a structured description and interpretation of immersive learning cases. The method is then demonstrated on a published immersive learning case on training for wind turbine maintenance using virtual reality. Applying the method results in a structured artifact, the Immersive Learning Case Sheet, that tags the case with its proximal uses, practices, and strategies, and refines the free text case description to ensure that matching details are included. This contribution is thus a case description method in support of future comparative research of immersive learning cases. We then discuss how the resulting description and interpretation can be leveraged to change immersion learning cases, by enriching them (considering low-effort changes or additions) or innovating (exploring more challenging avenues of transformation). The method holds significant promise to support better-grounded research in immersive learning.
Recently uploaded (20)
Authoring a personal GPT for your research and practice: How we created the Q...
Authoring a personal GPT for your research and practice: How we created the Q...
Sharlene Leurig - Enabling Onsite Water Use with Net Zero Water
Sharlene Leurig - Enabling Onsite Water Use with Net Zero Water
EWOCS-I: The catalog of X-ray sources in Westerlund 1 from the Extended Weste...
EWOCS-I: The catalog of X-ray sources in Westerlund 1 from the Extended Weste...
Equivariant neural networks and representation theory
Equivariant neural networks and representation theory
The use of Nauplii and metanauplii artemia in aquaculture (brine shrimp).pptx
The use of Nauplii and metanauplii artemia in aquaculture (brine shrimp).pptx
aziz sancar nobel prize winner: from mardin to nobel
aziz sancar nobel prize winner: from mardin to nobel
20240520 Planning a Circuit Simulator in JavaScript.pptx
20240520 Planning a Circuit Simulator in JavaScript.pptx
Unlocking the mysteries of reproduction: Exploring fecundity and gonadosomati...
Unlocking the mysteries of reproduction: Exploring fecundity and gonadosomati...
The cost of acquiring information by natural selection
The cost of acquiring information by natural selection
The debris of the ‘last major merger’ is dynamically young
The debris of the ‘last major merger’ is dynamically young
The binding of cosmological structures by massless topological defects
The binding of cosmological structures by massless topological defects
THEMATIC APPERCEPTION TEST(TAT) cognitive abilities, creativity, and critic...
THEMATIC APPERCEPTION TEST(TAT) cognitive abilities, creativity, and critic...
ESA/ACT Science Coffee: Diego Blas - Gravitational wave detection with orbita...
ESA/ACT Science Coffee: Diego Blas - Gravitational wave detection with orbita...
mô tả các thí nghiệm về đánh giá tác động dòng khí hóa sau đốt
mô tả các thí nghiệm về đánh giá tác động dòng khí hóa sau đốt
Remote Sensing and Computational, Evolutionary, Supercomputing, and Intellige...
Remote Sensing and Computational, Evolutionary, Supercomputing, and Intellige...
8.Isolation of pure cultures and preservation of cultures.pdf
8.Isolation of pure cultures and preservation of cultures.pdf
Describing and Interpreting an Immersive Learning Case with the Immersion Cub...
Describing and Interpreting an Immersive Learning Case with the Immersion Cub...
Proteins
- 1. Topic- proteins MS. AAFREEN KHANAM ASST. PROF. (DEPARTMENT OF MICROBIOLOGY) SHRI SHANKARACHARYA MAHAVIDYALAYA, JUNWANI BHILAI
- 2. Synopsis • Introduction • Definition • Functions of Proteins • Classification of Proteins • Structure of Proteins • Properties of Proteins • References
- 3. Introduction The term protein is derived from a Greek word proteios meaning holding the first place. Protein are the most abundant organic molecule of living systems. They occur in every part of the cell and constitutive about 50% of the cellular dry weight. Proteins form the fundamental basis of structure and functional unit of life. Unlike lipids and carbohydrates, proteins are not stored, so they must be consumed daily. Current recommended daily intake for adults is 0.8 grams of protein per kg of body weight (more is needed for children). Dietary protein comes from eating meat and milk.
- 7. Structure of proteins There are four levels of protein structure (primary, secondary, tertiary and quaternary). Primary structure: The primary structure of a protein is its unique sequence of amino acids. – Lysozyme, an enzyme that attacks bacteria, consists of a polypeptide chain of 129 amino acids. – The precise primary structure of a protein is determined by inherited genetic information. – At one end is an amino acid with a free amino group the (the N-terminus) and at the other is an amino acid with a free carboxyl group the (the C- terminus).
- 8. 2 Secondary structure: Results from hydrogen bond formation between hydrogen of –NH group of peptide bond and the carbonyl oxygen of another peptide bond. According to H-bonding there are two main forms of secondary structure: α-helix: It is a spiral structure resulting from hydrogen bonding between one peptide bond and the fourth one β-sheets: is another form of secondary structure in which two or more polypeptides (or segments of the same peptide chain) are linked together by hydrogen bond between H- of NH- of one chain and carbonyl oxygen of adjacent chain (or segment).
- 9. Tertiary structure is determined by a variety of interactions (bond formation) among R groups and between R groups and the polypeptide backbone. a. The weak interactions include: Hydrogen bonds among polar side chains Ionic bonds between charged R groups ( basic and acidic amino acids) Hydrophobic interactions among hydrophobic ( non polar) R groups.
- 10. b. Strong covalent bonds include disulfide bridges, that form between the sulfhydryl groups (SH) of cysteine monomers, stabilize the structure.
- 11. Quaternary structure: results from the aggregation (combination) of two or more polypeptide subunits held together by non-covalent interaction like H-bonds, ionic or hydrophobic interactions. Examples on protein having quaternary structure: Collagen is a fibrous protein of three polypeptides (trimeric) that are supercoiled like a rope.This provides the structural strength for their role in connective tissue. Hemoglobin is a globular protein with four polypeptide chains (tetrameric) Insulin : two polypeptide chains (dimeric)
- 13. Properties of proteins Solubility Molecular weight Shape Acidic and Basic amino acids Precipitation of Protein Colour reaction of protein
- 14. References Biochemistry by U.Satyanarayana Biochemistry by J. L. Jain. Lehninger Principles of Biochemistry by David L. Nelson and Michael M. Cox. Microbiology by Powar and Daginawala.