Protein structure levels
•Download as PPT, PDF•
8 likes•7,528 views
There are four levels of protein structure: 1) Primary structure is the linear sequence of amino acids linked by peptide bonds 2) Secondary structure involves folding due to hydrogen bonds between amino and acid groups, forming structures like alpha helices or beta sheets 3) Tertiary structure is the three dimensional folded structure resulting from attractions and repulsions between the R groups of the amino acids 4) Quaternary structure is the association of two or more protein chains, such as hemoglobin which is composed of four protein chains.
Report
Share
Report
Share
Recommended
Nucleotides an introduction
Nucleotides are the basic building blocks of nucleic acids like DNA and RNA. They consist of three components: a nitrogenous base, a pentose sugar, and a phosphate group. The nitrogenous bases include purines like adenine and guanine, and pyrimidines like cytosine and thymine in DNA or uracil in RNA. The pentose sugars are either deoxyribose in DNA or ribose in RNA. Successive nucleotides are linked by phosphodiester bonds between the phosphate group of one nucleotide and the hydroxyl group of the next. This forms the hydrophilic backbone of nucleic acids and gives them polarity with distinct 5' and 3' ends. The specific hydrogen bonding between nucleotide base pairs
Protein sturucture
This document discusses protein structure and function. It begins by defining proteins and their essential roles in the human body. It then describes the general characteristics of proteins, such as their chemical composition and functions. The document classifies proteins based on their composition, axial ratio, and biological functions. It explains the different levels of protein structure from primary to quaternary, focusing on secondary structure elements like alpha helices and beta sheets. The roles of hydrogen bonding, disulfide bridges, and ionic bonds in tertiary and quaternary structure are also described.
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.
Amino acids and protein
Proteins are macromolecules composed of amino acid subunits linked by peptide bonds. There are 20 common amino acids that make up proteins. Amino acids are classified based on properties like charge, polarity, and essentiality. Proteins form through peptide bond formation between amino acid residues, resulting in primary, secondary, tertiary, and quaternary structure levels that determine a protein's shape and function.
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.
Four levels of protein structure
A comprehensive presentation on Four levels of protein structure for MBBS, BDS, B Pharm & Biotechnology students to facilitate self- study.
SERINE & THREONINE METABOLISM
Serine is a non-essential amino acid that can be synthesized from glycolysis intermediates. It participates in one-carbon metabolism by donating methylene groups, and it is involved in the synthesis of several other amino acids, phospholipids, and sphingolipids. Serine can be converted to pyruvate through transamination and deamination reactions. Threonine is an essential amino acid that can be cleaved to form glycine, acetaldehyde, and derivatives that enter the citric acid cycle or form pyruvate and lactate. Both amino acids play important roles in biosynthesis as carriers of phosphate groups.
BIOSYNTHESIS OF FATTY ACIDS
This document summarizes the process of de novo fatty acid synthesis. It occurs in the cytosol of liver, kidney, adipose tissue, and lactating mammary glands. Acetyl-CoA is the starting material, which is transported from mitochondria to the cytosol via citrate. In the cytosol, fatty acid synthase complex catalyzes the reactions to produce palmitic acid (C16) through cycles of condensation, reduction, dehydration, and reduction. The process requires acetyl-CoA, malonyl-CoA, ATP, and NADPH as substrates and is regulated by enzymes and hormones.
Recommended
Nucleotides an introduction
Nucleotides are the basic building blocks of nucleic acids like DNA and RNA. They consist of three components: a nitrogenous base, a pentose sugar, and a phosphate group. The nitrogenous bases include purines like adenine and guanine, and pyrimidines like cytosine and thymine in DNA or uracil in RNA. The pentose sugars are either deoxyribose in DNA or ribose in RNA. Successive nucleotides are linked by phosphodiester bonds between the phosphate group of one nucleotide and the hydroxyl group of the next. This forms the hydrophilic backbone of nucleic acids and gives them polarity with distinct 5' and 3' ends. The specific hydrogen bonding between nucleotide base pairs
Protein sturucture
This document discusses protein structure and function. It begins by defining proteins and their essential roles in the human body. It then describes the general characteristics of proteins, such as their chemical composition and functions. The document classifies proteins based on their composition, axial ratio, and biological functions. It explains the different levels of protein structure from primary to quaternary, focusing on secondary structure elements like alpha helices and beta sheets. The roles of hydrogen bonding, disulfide bridges, and ionic bonds in tertiary and quaternary structure are also described.
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.
Amino acids and protein
Proteins are macromolecules composed of amino acid subunits linked by peptide bonds. There are 20 common amino acids that make up proteins. Amino acids are classified based on properties like charge, polarity, and essentiality. Proteins form through peptide bond formation between amino acid residues, resulting in primary, secondary, tertiary, and quaternary structure levels that determine a protein's shape and function.
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.
Four levels of protein structure
A comprehensive presentation on Four levels of protein structure for MBBS, BDS, B Pharm & Biotechnology students to facilitate self- study.
SERINE & THREONINE METABOLISM
Serine is a non-essential amino acid that can be synthesized from glycolysis intermediates. It participates in one-carbon metabolism by donating methylene groups, and it is involved in the synthesis of several other amino acids, phospholipids, and sphingolipids. Serine can be converted to pyruvate through transamination and deamination reactions. Threonine is an essential amino acid that can be cleaved to form glycine, acetaldehyde, and derivatives that enter the citric acid cycle or form pyruvate and lactate. Both amino acids play important roles in biosynthesis as carriers of phosphate groups.
BIOSYNTHESIS OF FATTY ACIDS
This document summarizes the process of de novo fatty acid synthesis. It occurs in the cytosol of liver, kidney, adipose tissue, and lactating mammary glands. Acetyl-CoA is the starting material, which is transported from mitochondria to the cytosol via citrate. In the cytosol, fatty acid synthase complex catalyzes the reactions to produce palmitic acid (C16) through cycles of condensation, reduction, dehydration, and reduction. The process requires acetyl-CoA, malonyl-CoA, ATP, and NADPH as substrates and is regulated by enzymes and hormones.
Protein Structure and Function
The document discusses protein structure and function. It describes the basic building blocks of proteins, amino acids, and how they combine to form the primary structure. It then explains how the primary structure can take on regular patterns called secondary structures, including alpha helices and beta sheets. Alpha helices form coiled structures stabilized by hydrogen bonds between amino acids, while beta sheets involve hydrogen bonding between peptide chains to form extended structures. The precise sequence and folding of a protein's amino acids determines its final three-dimensional shape and function.
Lec 11 level 3-de (genetic code and protein biosynthesis)
This document discusses RNA and protein biosynthesis. It describes the key types of RNA - mRNA, tRNA, and rRNA. mRNA carries DNA's genetic message to the ribosome for protein synthesis. tRNA transfers amino acids to the ribosome. rRNA provides the infrastructure for mRNA, tRNA and amino acids to interact during translation. The central dogma of molecular biology is that DNA's genetic information is transcribed into mRNA and then translated into protein. The genetic code uses triplet codons to specify each amino acid. Inhibitors like actinomycin D and streptomycin can block RNA and protein synthesis in bacteria.
Physical properties of Carbohydrates
The document discusses the physical properties of carbohydrates including monosaccharides, disaccharides, and polysaccharides. Monosaccharides are the simplest sugars and include glucose, fructose, and galactose. Disaccharides are formed when two monosaccharides join together, such as sucrose, lactose, and maltose. Polysaccharides have long chains of monosaccharide units and include starch, glycogen, cellulose, and chitin. The properties of carbohydrates differ based on their size, from monosaccharides being the smallest and most soluble to polysaccharides having more complex structures and being less soluble.
Acid –Base Properties of Amino Acids
- Amino acids exist in two forms, L and D, depending on their stereoisomer configuration. Only L-amino acids are used in protein synthesis.
- Amino acids are amphoteric, meaning they can act as acids or bases depending on the pH. At low pH they are protonated and at high pH they are deprotonated.
- In solution, amino acids exist as zwitterions - molecules with both positive and negative charges that cancel out to have no overall charge. The isoelectric point is the pH at which the zwitterion form dominates.
Structure of protein
This document summarizes the four levels of protein structure: primary, secondary, tertiary, and quaternary. It provides details on each level: primary structure refers to the linear sequence of amino acids in the polypeptide chain. Secondary structure involves hydrogen bonding between amino acids to form regular structures like alpha helices and beta pleated sheets. Tertiary structure describes the overall 3D shape of the protein arising from secondary structures. Quaternary structure involves interactions between two or more polypeptide chains, as seen in hemoglobin which is made of four polypeptide subunits.
Peptides
Peptides are short chains of amino acids linked by peptide bonds. They are distinguished from proteins by typically containing fewer than 50 amino acid units. Peptides are formed through condensation reactions between carboxyl and amino groups of separate amino acids, releasing a water molecule. Peptide bonds are rigid and planar, contributing to protein structure stability. Peptides serve many important biological functions and can be classified based on their production method, including through ribosomal translation, nonribosomal synthesis, and enzymatic digestion of proteins in foods. Bioactive peptides derived from food proteins can have beneficial effects like lowering blood pressure, cholesterol, and antimicrobial properties.
Determination of primary structure of proteins
The document discusses the determination of the primary structure of proteins. It begins by explaining that proteins are composed of amino acid residues linked by peptide bonds to form a polypeptide chain. The primary structure refers to the specific sequence of amino acids in this chain. Mass spectrometry and tandem mass spectrometry techniques are used to analyze protein fragments obtained through enzymatic or chemical cleavage to determine the amino acid sequence and thereby elucidate the primary structure.
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.
Chemistry of nucleotides
- Nucleotides are composed of a nitrogenous base (purine or pyrimidine), a pentose sugar (ribose or deoxyribose), and one or more phosphate groups. When a base combines with a sugar, a nucleoside is formed. The addition of phosphate groups forms nucleotides.
- The four bases found in nucleic acids are adenine, guanine, cytosine, and either thymine in DNA or uracil in RNA. These bases combine with either ribose or deoxyribose to form nucleosides like AMP, GMP, CMP, TMP, or UMP.
- Nucleotides are the monomers that make up nucleic acids DNA and RNA
Structure of proteins
Gives in detail primary, secondary, tertiary and Quaternary structure of proteins. Gives classification of secondary structure: alpha helix, beta pleated sheet and different types of tight turns and explains most commonly found tight turn in proteins i.e. beta turn. Briefs about the Ramachandran plot of proteins, dihedral or torsion angles and explains why glycine and proline act as alpha helix breakers. Explains tertiary structure of proteins and different covalent and non covalent bonds in the tertiary structure and relative importance of these bonding interactions. Details about the quaternary structure of proteins and explains why hemoglobin is a quaternary protein and insulin is not.
Amino acid catabolism- Part-1
Formation and fate of Ammonia
Transdeamination, oxidative and non oxidative deamination, Ammonia transport, Ammonia intoxication, Ammonia detoxification
Amino acid and protein chemistery
Proteins are the most abundant and functionally diverse molecules in living systems, composed of amino acids linked by peptide bonds. They can be classified in various ways, including by molecular structure (globular vs fibrous), solubility, presence of non-protein groups, function (enzymes, hormones, etc.), and nutritional quality. The 20 primary amino acids are the building blocks of all proteins in plants and animals, and each has a specific genetic codon in mRNA.
Chapter 3(part1) - Amino acids, peptides, and proteins
website: http://www.am-medicine.com
Facebook page : https://www.facebook.com/pages/Am-medicine/207726329406832
Facebook group: https://www.facebook.com/groups/1409138472653811/
Primary and Secondary Structure of Protein
The document discusses the primary structure of proteins, which refers to the specific sequence of amino acids in a polypeptide chain. Amino acids are linked together by peptide bonds to form the primary structure. The different arrangements of amino acids give rise to different protein structures and functions. The primary structure determines the overall shape and conformation of a protein.
BIOSYNTHESIS OF PURINE NUCLEOTIDES
1. The document summarizes purine nucleotide synthesis, which involves multiple enzymatic reactions using substrates like aspartate, glutamine, glycine, and CO2 to build the purine ring structure on ribose 5-phosphate.
2. Liver is the major site of de novo purine synthesis, while erythrocytes and brain must salvage purines due to their inability to synthesize them.
3. Feedback inhibition regulates purine synthesis at committed steps, and analogs like 6-mercaptopurine can inhibit pathways leading to AMP and GMP formation.
lipid clinical importance sdk 2013
Compound lipids contain additional substances like phosphorus, carbohydrates or proteins in addition to fatty acids and alcohols. Phospholipids are important compound lipids that contain phosphoric acid and make up cell membranes. They are classified as glycerophospholipids containing glycerol or sphingophospholipids containing sphingosine. Glycolipids contain carbohydrate residues and sphingosine. Lipoproteins combine lipids and proteins and transport lipids in the bloodstream, classified by density.
Structure and functions of glycoplipids and glycoproteins
Glycoproteins and glycolipids are glycoconjugates that contain carbohydrate chains covalently bonded to lipids or proteins. Glycolipids are composed of a monosaccharide unit joined to a hydrophobic lipid moiety, forming amphiphilic molecules that aggregate in aqueous environments into bilayers, micelles, or lamellar structures. Glycoproteins can be O-linked via hydroxyl side chains of serine or threonine or N-linked via amide nitrogen of asparagine. Glycoproteins function in secretions, cell membranes, and as receptors. Abnormalities in glycoconjugate synthesis can lead to diseases like cancer metastasis.
Biochemistry 2
Biochemistry studies the chemical structures and processes in living organisms. It has revolutionized the biological sciences by explaining life in terms of fundamental chemical and physical principles. Biochemistry is an interdisciplinary field that incorporates organic chemistry, biophysics, genetics and more to study the molecules that make up cells such as proteins, carbohydrates and nucleic acids and how they enable the basic functions of life.
Amino acid ppt
There are 20 common amino acids that serve as the building blocks of proteins. Amino acids contain an amino group, a carboxyl group, and a variable side chain. They join together through peptide bonds to form polypeptides and proteins. Ten of the 20 amino acids are considered essential and must be obtained through diet as humans cannot synthesize them. Proteins perform a wide variety of important functions in the body.
PROTEINS
This document discusses proteins, including their definition, composition, sources, storage, requirements, functions, structure, and classification. Some key points:
- Proteins are polypeptides composed of amino acids joined by peptide bonds. They are essential to life and perform many catalytic, structural, transport, and other functions.
- Sources of proteins include animal sources like meat and dairy as well as plant sources like legumes. Storage capacity in organisms is limited compared to carbohydrates and fats.
- Proteins are classified based on their nutritional value, function, structure, and physicochemical properties. Complete proteins contain all essential amino acids while incomplete proteins lack some.
- Structure depends on shape - globular
Lecture 2 3 protein chemistry
Proteins are composed of amino acids linked by peptide bonds. They 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. Tertiary structure is the overall 3D shape formed by interactions between secondary structures. Quaternary structure refers to the arrangement of multiple polypeptide subunits in a protein.
Chemistry of amino acids with their clinical applications
A comprehensive presentation on Chemistry of Amino acids with their clinical applications for MBBS , BDS, B Pharm & Biotechnology students to facilitate easy- learning.
More Related Content
What's hot
Protein Structure and Function
The document discusses protein structure and function. It describes the basic building blocks of proteins, amino acids, and how they combine to form the primary structure. It then explains how the primary structure can take on regular patterns called secondary structures, including alpha helices and beta sheets. Alpha helices form coiled structures stabilized by hydrogen bonds between amino acids, while beta sheets involve hydrogen bonding between peptide chains to form extended structures. The precise sequence and folding of a protein's amino acids determines its final three-dimensional shape and function.
Lec 11 level 3-de (genetic code and protein biosynthesis)
This document discusses RNA and protein biosynthesis. It describes the key types of RNA - mRNA, tRNA, and rRNA. mRNA carries DNA's genetic message to the ribosome for protein synthesis. tRNA transfers amino acids to the ribosome. rRNA provides the infrastructure for mRNA, tRNA and amino acids to interact during translation. The central dogma of molecular biology is that DNA's genetic information is transcribed into mRNA and then translated into protein. The genetic code uses triplet codons to specify each amino acid. Inhibitors like actinomycin D and streptomycin can block RNA and protein synthesis in bacteria.
Physical properties of Carbohydrates
The document discusses the physical properties of carbohydrates including monosaccharides, disaccharides, and polysaccharides. Monosaccharides are the simplest sugars and include glucose, fructose, and galactose. Disaccharides are formed when two monosaccharides join together, such as sucrose, lactose, and maltose. Polysaccharides have long chains of monosaccharide units and include starch, glycogen, cellulose, and chitin. The properties of carbohydrates differ based on their size, from monosaccharides being the smallest and most soluble to polysaccharides having more complex structures and being less soluble.
Acid –Base Properties of Amino Acids
- Amino acids exist in two forms, L and D, depending on their stereoisomer configuration. Only L-amino acids are used in protein synthesis.
- Amino acids are amphoteric, meaning they can act as acids or bases depending on the pH. At low pH they are protonated and at high pH they are deprotonated.
- In solution, amino acids exist as zwitterions - molecules with both positive and negative charges that cancel out to have no overall charge. The isoelectric point is the pH at which the zwitterion form dominates.
Structure of protein
This document summarizes the four levels of protein structure: primary, secondary, tertiary, and quaternary. It provides details on each level: primary structure refers to the linear sequence of amino acids in the polypeptide chain. Secondary structure involves hydrogen bonding between amino acids to form regular structures like alpha helices and beta pleated sheets. Tertiary structure describes the overall 3D shape of the protein arising from secondary structures. Quaternary structure involves interactions between two or more polypeptide chains, as seen in hemoglobin which is made of four polypeptide subunits.
Peptides
Peptides are short chains of amino acids linked by peptide bonds. They are distinguished from proteins by typically containing fewer than 50 amino acid units. Peptides are formed through condensation reactions between carboxyl and amino groups of separate amino acids, releasing a water molecule. Peptide bonds are rigid and planar, contributing to protein structure stability. Peptides serve many important biological functions and can be classified based on their production method, including through ribosomal translation, nonribosomal synthesis, and enzymatic digestion of proteins in foods. Bioactive peptides derived from food proteins can have beneficial effects like lowering blood pressure, cholesterol, and antimicrobial properties.
Determination of primary structure of proteins
The document discusses the determination of the primary structure of proteins. It begins by explaining that proteins are composed of amino acid residues linked by peptide bonds to form a polypeptide chain. The primary structure refers to the specific sequence of amino acids in this chain. Mass spectrometry and tandem mass spectrometry techniques are used to analyze protein fragments obtained through enzymatic or chemical cleavage to determine the amino acid sequence and thereby elucidate the primary structure.
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.
Chemistry of nucleotides
- Nucleotides are composed of a nitrogenous base (purine or pyrimidine), a pentose sugar (ribose or deoxyribose), and one or more phosphate groups. When a base combines with a sugar, a nucleoside is formed. The addition of phosphate groups forms nucleotides.
- The four bases found in nucleic acids are adenine, guanine, cytosine, and either thymine in DNA or uracil in RNA. These bases combine with either ribose or deoxyribose to form nucleosides like AMP, GMP, CMP, TMP, or UMP.
- Nucleotides are the monomers that make up nucleic acids DNA and RNA
Structure of proteins
Gives in detail primary, secondary, tertiary and Quaternary structure of proteins. Gives classification of secondary structure: alpha helix, beta pleated sheet and different types of tight turns and explains most commonly found tight turn in proteins i.e. beta turn. Briefs about the Ramachandran plot of proteins, dihedral or torsion angles and explains why glycine and proline act as alpha helix breakers. Explains tertiary structure of proteins and different covalent and non covalent bonds in the tertiary structure and relative importance of these bonding interactions. Details about the quaternary structure of proteins and explains why hemoglobin is a quaternary protein and insulin is not.
Amino acid catabolism- Part-1
Formation and fate of Ammonia
Transdeamination, oxidative and non oxidative deamination, Ammonia transport, Ammonia intoxication, Ammonia detoxification
Amino acid and protein chemistery
Proteins are the most abundant and functionally diverse molecules in living systems, composed of amino acids linked by peptide bonds. They can be classified in various ways, including by molecular structure (globular vs fibrous), solubility, presence of non-protein groups, function (enzymes, hormones, etc.), and nutritional quality. The 20 primary amino acids are the building blocks of all proteins in plants and animals, and each has a specific genetic codon in mRNA.
Chapter 3(part1) - Amino acids, peptides, and proteins
website: http://www.am-medicine.com
Facebook page : https://www.facebook.com/pages/Am-medicine/207726329406832
Facebook group: https://www.facebook.com/groups/1409138472653811/
Primary and Secondary Structure of Protein
The document discusses the primary structure of proteins, which refers to the specific sequence of amino acids in a polypeptide chain. Amino acids are linked together by peptide bonds to form the primary structure. The different arrangements of amino acids give rise to different protein structures and functions. The primary structure determines the overall shape and conformation of a protein.
BIOSYNTHESIS OF PURINE NUCLEOTIDES
1. The document summarizes purine nucleotide synthesis, which involves multiple enzymatic reactions using substrates like aspartate, glutamine, glycine, and CO2 to build the purine ring structure on ribose 5-phosphate.
2. Liver is the major site of de novo purine synthesis, while erythrocytes and brain must salvage purines due to their inability to synthesize them.
3. Feedback inhibition regulates purine synthesis at committed steps, and analogs like 6-mercaptopurine can inhibit pathways leading to AMP and GMP formation.
lipid clinical importance sdk 2013
Compound lipids contain additional substances like phosphorus, carbohydrates or proteins in addition to fatty acids and alcohols. Phospholipids are important compound lipids that contain phosphoric acid and make up cell membranes. They are classified as glycerophospholipids containing glycerol or sphingophospholipids containing sphingosine. Glycolipids contain carbohydrate residues and sphingosine. Lipoproteins combine lipids and proteins and transport lipids in the bloodstream, classified by density.
Structure and functions of glycoplipids and glycoproteins
Glycoproteins and glycolipids are glycoconjugates that contain carbohydrate chains covalently bonded to lipids or proteins. Glycolipids are composed of a monosaccharide unit joined to a hydrophobic lipid moiety, forming amphiphilic molecules that aggregate in aqueous environments into bilayers, micelles, or lamellar structures. Glycoproteins can be O-linked via hydroxyl side chains of serine or threonine or N-linked via amide nitrogen of asparagine. Glycoproteins function in secretions, cell membranes, and as receptors. Abnormalities in glycoconjugate synthesis can lead to diseases like cancer metastasis.
Biochemistry 2
Biochemistry studies the chemical structures and processes in living organisms. It has revolutionized the biological sciences by explaining life in terms of fundamental chemical and physical principles. Biochemistry is an interdisciplinary field that incorporates organic chemistry, biophysics, genetics and more to study the molecules that make up cells such as proteins, carbohydrates and nucleic acids and how they enable the basic functions of life.
Amino acid ppt
There are 20 common amino acids that serve as the building blocks of proteins. Amino acids contain an amino group, a carboxyl group, and a variable side chain. They join together through peptide bonds to form polypeptides and proteins. Ten of the 20 amino acids are considered essential and must be obtained through diet as humans cannot synthesize them. Proteins perform a wide variety of important functions in the body.
PROTEINS
This document discusses proteins, including their definition, composition, sources, storage, requirements, functions, structure, and classification. Some key points:
- Proteins are polypeptides composed of amino acids joined by peptide bonds. They are essential to life and perform many catalytic, structural, transport, and other functions.
- Sources of proteins include animal sources like meat and dairy as well as plant sources like legumes. Storage capacity in organisms is limited compared to carbohydrates and fats.
- Proteins are classified based on their nutritional value, function, structure, and physicochemical properties. Complete proteins contain all essential amino acids while incomplete proteins lack some.
- Structure depends on shape - globular
What's hot (20)
Lec 11 level 3-de (genetic code and protein biosynthesis)
Lec 11 level 3-de (genetic code and protein biosynthesis)
Chapter 3(part1) - Amino acids, peptides, and proteins
Chapter 3(part1) - Amino acids, peptides, and proteins
Structure and functions of glycoplipids and glycoproteins
Structure and functions of glycoplipids and glycoproteins
Similar to Protein structure levels
Lecture 2 3 protein chemistry
Proteins are composed of amino acids linked by peptide bonds. They 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. Tertiary structure is the overall 3D shape formed by interactions between secondary structures. Quaternary structure refers to the arrangement of multiple polypeptide subunits in a protein.
Chemistry of amino acids with their clinical applications
A comprehensive presentation on Chemistry of Amino acids with their clinical applications for MBBS , BDS, B Pharm & Biotechnology students to facilitate easy- learning.
Lecture 2 3 protein chemistry
Proteins are composed of amino acids linked by 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 structures form based on hydrogen bonding patterns between amino acids. The two main secondary structures are the alpha helix, where amino acids coil into a helical shape, and the beta sheet, where amino acids align into beta strands connected by hydrogen bonds.
Lecture 2 3 protein chemistry
Proteins are composed of amino acids linked by peptide bonds. There are four levels of protein structure - primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. The two most common types of secondary structure are the alpha helix and beta sheet. In an alpha helix, amino acid residues form a coil stabilized by hydrogen bonds between residues four places apart in the sequence. In a beta sheet, residues form extended zigzag patterns stabilized by hydrogen bonds between residues on adjacent strands running in parallel or anti-parallel directions.
Lecture 2 3 protein chemistry
Proteins are composed of amino acids linked by peptide bonds. They have four levels of structure - primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Common secondary structures are alpha helices and beta sheets formed by hydrogen bonding between amino acids. Tertiary structure refers to the overall 3D structure formed from secondary structures. Quaternary structure involves interactions between multiple polypeptide subunits.
protiens
Proteins are composed of amino acids linked together in chains. There are 20 common amino acids that make up proteins and each contains different functional groups. A protein's function depends on both its amino acid composition and sequence. Proteins fold into complex 3D shapes like spheres, strands, and sheets. All the information to determine a protein's 3D structure is contained in its linear amino acid sequence. There are essential and non-essential amino acids for human nutrition. Peptides are short chains of amino acids while proteins are longer chains that can assemble into complex structures like alpha helices and beta sheets at the primary, secondary, tertiary, and quaternary levels.
Amino-acids-and-protein..ppt
Amino acids are the building blocks of proteins. There are 20 standard amino acids that make up the proteins in living organisms. Amino acids contain an amino group and a carboxyl group, and can be joined together via peptide bonds to form polypeptide chains. Proteins have complex structures with four levels of organization - primary, secondary, tertiary, and quaternary structure. The primary structure is the linear sequence of amino acids in the polypeptide chain. Secondary structures include alpha helices and beta sheets formed from regular patterns of hydrogen bonds between amino acids in the chain.
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.
Amino acid sdk (biochem)
Amino acids are organic compounds that contain an amino group and a carboxyl group. There are over 300 amino acids found in nature, but only 20 are used as building blocks of proteins in the body. Each amino acid contains an alpha carbon atom bonded to an amino group, a carboxyl group, a hydrogen atom, and a unique side chain. At physiological pH, amino acids exist as zwitterions with both positive and negative charges. Amino acids join together via peptide bonds to form polypeptides and proteins. The 20 standard amino acids are classified based on properties like polarity and acidity of their side chains. Amino acids and proteins are essential for building body tissues and important biomolecules like enzymes, hormones
AMINO ACIDS AND PEPTIDES.pdf
The document discusses amino acids and peptides. It provides information on:
1. The structure and properties of the 20 common amino acids found in proteins, including their ionization states and isoelectric points.
2. How amino acids can act as acids or bases depending on pH due to ionization of their carboxyl and amino groups.
3. The formation of peptide bonds between amino acids and how this leads to the creation of polypeptides and proteins of physiological significance.
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.
219101 lecture 6
This document provides an overview of protein structure and function. It discusses the four levels of protein structure from primary to quaternary structure. The 20 standard amino acids that serve as building blocks of proteins are described in terms of their chemical and physical properties. Amino acids contain both polar and non-polar side chains that influence protein structure and function. Key concepts covered include protein folding, the zwitterionic nature of amino acids, and interactions like disulfide bonds and hydrophobic effects that stabilize protein tertiary structure.
Amino acids.ppt
This document discusses the structure and classification of amino acids. It begins by stating that amino acids are the basic structural units of proteins and that there are 20 standard amino acids found in protein structures. The general structure of an amino acid is presented, showing that they contain an amino group, a carboxyl group, and a variable R group (side chain) attached to the alpha carbon. Amino acids are then classified into four types based on the polarity of their R groups: non-polar aliphatic, non-polar aromatic, polar uncharged, and polar charged (acidic or basic). Examples of amino acids that fall into each of these four categories are provided.
Chemistry Notes on Amino acids class 12.pdf
1. Amino acids are organic compounds that contain amino and carboxyl groups and form proteins through peptide bonds. There are essential and non-essential amino acids.
2. In aqueous solutions, amino acids exist as zwitterions with both positive and negative charges which allows them to react as both acids and bases.
Amino Acids.pptx
This document discusses amino acids, which are organic compounds that contain amino and carboxyl groups and form proteins by binding together via peptide bonds. Amino acids are classified based on their structure, polarity, and nutritional requirements. There are essential and non-essential amino acids. Amino acids can undergo reactions like decarboxylation, amide formation, transamination, and oxidative deamination. They have amphoteric properties due to acidic and basic groups and exist as zwitterions at their isoelectric pH. Peptide bonds between amino acids are planar and rigid.
H ydrocarbon I
This document discusses aliphatic hydrocarbons, specifically alkanes. It begins by introducing hydrocarbons and classifying them as either aliphatic or aromatic. Alkanes, also known as paraffins, are saturated aliphatic hydrocarbons that have the general formula CnH2n+2. The simplest alkane is methane, and higher alkanes like ethane, propane, and butane make up homologous series where the molecular formula differs by CH2. Alkanes can exhibit isomerism where compounds have the same molecular formula but different structural arrangements and properties.
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.
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.
Proteins
This document discusses proteins and their structure. It begins by introducing proteins and their composition of amino acids linked into peptide chains. It then describes the 20 main amino acids and how they are classified. The four levels of protein structural organization - primary, secondary, tertiary, and quaternary structure - are outlined. Common secondary structures like the alpha helix and beta sheet are also defined. Specific proteins like hemoglobin and myoglobin are then examined in more detail, including their subunit composition and role in oxygen transport.
Proteins ppt
Protein is an important component of every cell in the body. Hair and nails are mostly made of protein. Your body uses protein to build and repair tissues. You also use protein to make enzymes, hormones, and other body chemicals. Protein is an important building block of bones, muscles, cartilage, skin, and blood.
Similar to Protein structure levels (20)
Chemistry of amino acids with their clinical applications
Chemistry of amino acids with their clinical applications
More from Sabahat Ali
RECOMBINATION MOLECULAR BIOLOGY PPT UPDATED new.pptx
This ppt is about recombination and where it occurs. Types of recombination and models of recombination along with many factors in prokaryotic and eukaryotic recombination
Good laboratory practices in a pharmaceutical lab 1
This document discusses good laboratory practices in a pharmaceutical lab. It outlines the members of a group project on this topic and provides an introduction to pharmaceutical lab testing. It then covers topics like GMP, GLP, quality control, quality assurance, reducing human errors, and the scope of QA and QC in a pharmaceutical lab. Key points include that pharmaceutical labs test raw materials, finished products, and conduct validation, stability, and analytical method development testing. GMP and GLP aim to minimize risks and ensure consistent quality production. QA and QC work to guarantee drug quality and safety at all stages from development to sales.
Degradation of PLA at Mesophillic and thermophillic conditions
This document summarizes research on the degradation of polylactic acid (PLA) under mesophilic and thermophilic conditions. Key findings include:
1) Mesophilic bacteria like Pseudomonas geniculata and Streptomyces pavanii were found to degrade PLA films at 25-40°C, with S. pavanii showing higher degradation.
2) PLA degradation was higher under thermophilic (41-122°C) conditions compared to mesophilic (20-45°C) due to PLA-degrading enzymes working best at high temperatures. Up to 90% of PLA weight loss was observed at thermophilic temperatures within 12 days of
Life cycle Assesment and waste stratigies of PLA
Group 2 presented on strategies for polylactic acid (PLA) waste, including recycling and biodegradation. There are three main routes for producing PLA: polymerization of lactic acid monomers, condensation of lactic acid, and fermentation. PLA can be chemically recycled through hydrolytic or alcoholytic depolymerization. An innovative process called the Zeus Waste PLA Depolymerization Process uses solvents like chloroform and alcohols like methanol at low temperatures to break PLA down into its original lactic acid monomers. PLA biodegrades through hydrolysis of ester bonds, thermal degradation, and photodegradation when exposed to sunlight.
Environmental biodegradation of PLA by Biotic and Abiotic factors
PLA is a biodegradable polymer that can degrade through both biotic and abiotic factors in the environment. Biotic degradation occurs through the action of microorganisms like bacteria and fungi that produce enzymes to break down PLA. Specific bacteria identified to degrade PLA include species of Pseudomonas and Streptomyces. Fungal degradation is also possible, with Phanerochaete chrysosporium shown to effectively degrade PLA. Abiotic degradation happens through hydrolysis when water breaks the ester bonds of PLA, which is accelerated at higher temperatures and pH levels.
Energy expenditure and BMR
The document discusses energy expenditure and basal metabolic rate (BMR). It defines energy expenditure as the amount of energy needed for bodily functions like breathing and circulation, while BMR is the minimum energy required for essential physiological processes when at rest. The document outlines several factors that affect BMR, such as age, gender, weight, and thyroid function. Maintaining caloric balance between intake and expenditure through diet and exercise can prevent weight gain.
Agriculture applications of nanobiotechnology
This document discusses the potential applications of nanobiotechnology in agriculture. It begins by introducing how nanoparticles can interact with agricultural hosts and tissues. It then discusses several specific applications, including using nanoparticles for plant disease management and diagnostics, as well as for delivering pesticides, nutrients, and plant hormones. The document also notes potential applications in areas like recycling agricultural waste, soil improvement, water purification, and plant breeding. It acknowledges both the promise and challenges of nanotechnology for modernizing agriculture to address issues like increasing food supply to support population growth amid changing environmental conditions.
Macronutrients and nutrition
Macronutrients provide energy and are essential for growth and maintenance of the body. The document discusses the three main macronutrients - carbohydrates, proteins, and fats. Carbohydrates are divided into simple and complex categories, with simple carbs like sugars providing quick energy and complex carbs like whole grains being more filling and nutritious. Proteins are essential building blocks and energy sources, with animal products providing complete proteins and plant sources providing complementary proteins when combined. Fats serve various functions in the body and are classified based on their structure.
Poly lactic Acid Biodegradation
The document discusses methods to enhance the biodegradation of polylactic acid (PLA). It analyzes modifications to PLA's physical properties and amending the environment with various factors like stimulants. It summarizes that biodegradation of PLA mainly occurs through hydrolysis of ester bonds and is induced by microorganisms like certain actinomycetes, bacteria, and fungi. Key factors like temperature, pH, humidity, and oxygen levels also affect the degradation rate. While PLA is biodegradable, the process is often slow under natural conditions.
Alzhemier's disease and koraskoff syndrome
Alzheimer's disease, Korsakoff's syndrome, and dreaming are compared and contrasted. Alzheimer's disease results from neuronal death and synapse loss, causing memory loss and dementia. Korsakoff's syndrome is caused by thiamine deficiency and can be reversed if treated early. Dreams occur during REM sleep and may help with memory consolidation. Both diseases involve memory loss and neuronal/synaptic changes, while dreaming is a normal process that occurs during sleep and differs in its effects on memory and brain activity.
Nerve cells, Nervous communication & its link to the celllular signalling
The document discusses the structure and function of neurons. It notes that neurons are specialized cells that communicate via electrical and chemical signals. They contain dendrites that receive signals, a cell body, and an axon that transmits signals. At synapses, chemical neurotransmitters transmit signals between neurons or to other cell types. Neurons form circuits that allow for complex coordinated responses. The action potential involves changes in ion channel permeability that propagate electrical signals rapidly along axons. Calcium acts as an important intracellular messenger in neurons and other cell types, often working through the calcium sensor protein calmodulin.
Peptide Hormones and Catecholamines
Peptide hormones and catecholamines allow for rapid responses to environmental changes. They are stored in secretory vesicles and released via exocytosis within seconds or minutes in response to stimulation. This causes short-term effects that are terminated once the hormones are degraded. In contrast, steroid hormones and thyroid hormones are synthesized from cholesterol or thyroglobulin precursors within cells. They diffuse out of cells and circulate in the blood bound to carrier proteins. This allows their effects to last longer, from hours to days, but production and release takes longer than for peptide hormones and catecholamines. The different hormone types thus allow for both rapid short-term responses and longer-term regulatory effects.
Membrane Proteins & its types
Integral & Peripheral membrane proteins
Helical membrane proteins could be single pass /multi pass
porins which are beta sheets ion channels.
membrane lipids & its types
lipids are categorized into 4 major categories.
1) phospholipids
2) glycolipids
3) steroids
4) archeal membrane lipids
Biomembranes (lipids, proteins, carbohydrates)
It includes composition of membranes (fluid mosaic model)
where these membranes are present?
what functions membranes perform?
cell to cell signalling
Cells in multicellular organisms communicate through elaborate signaling networks involving hundreds of signaling molecules. These molecules allow cells to regulate development, growth, and coordinated function. Signaling occurs through paracrine, synaptic, and endocrine mechanisms using molecules like hormones, neurotransmitters, and growth factors. Target cells contain receptors that recognize signaling molecules with high specificity and affinity. While some responses are rapid, others involve long-term changes through regulated synthesis, release, and degradation of signaling compounds.
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.
Proetin Tertiary Structure
Tertiary Structure basically of Hydrophobic interactions, (interactions in side chains), hydrogen bonding, salt bridges, Vander Waals interactions.
e.g. Globular proteins & Fibrous Proteins
Restriction digestion
Restriction Enzymes are used to digest DNA at specific Restriction sites(flanking ends) to produce ends that are either cohesive or blunt.
Polymerase Chain Reaction(PCR)
Amplifying DNA through polymerase chain reaction,
3 steps in PCR
Denaturation
Annealing
Extension
More from Sabahat Ali (20)
RECOMBINATION MOLECULAR BIOLOGY PPT UPDATED new.pptx
RECOMBINATION MOLECULAR BIOLOGY PPT UPDATED new.pptx
Good laboratory practices in a pharmaceutical lab 1
Good laboratory practices in a pharmaceutical lab 1
Degradation of PLA at Mesophillic and thermophillic conditions
Degradation of PLA at Mesophillic and thermophillic conditions
Environmental biodegradation of PLA by Biotic and Abiotic factors
Environmental biodegradation of PLA by Biotic and Abiotic factors
Nerve cells, Nervous communication & its link to the celllular signalling
Nerve cells, Nervous communication & its link to the celllular signalling
Recently uploaded
Bob Reedy - Nitrate in Texas Groundwater.pdf
Presented at June 6-7 Texas Alliance of Groundwater Districts Business Meeting
Deep Software Variability and Frictionless Reproducibility
Deep Software Variability and Frictionless ReproducibilityUniversity of Rennes, INSA Rennes, Inria/IRISA, CNRS
The ability to recreate computational results with minimal effort and actionable metrics provides a solid foundation for scientific research and software development. When people can replicate an analysis at the touch of a button using open-source software, open data, and methods to assess and compare proposals, it significantly eases verification of results, engagement with a diverse range of contributors, and progress. However, we have yet to fully achieve this; there are still many sociotechnical frictions.
Inspired by David Donoho's vision, this talk aims to revisit the three crucial pillars of frictionless reproducibility (data sharing, code sharing, and competitive challenges) with the perspective of deep software variability.
Our observation is that multiple layers — hardware, operating systems, third-party libraries, software versions, input data, compile-time options, and parameters — are subject to variability that exacerbates frictions but is also essential for achieving robust, generalizable results and fostering innovation. I will first review the literature, providing evidence of how the complex variability interactions across these layers affect qualitative and quantitative software properties, thereby complicating the reproduction and replication of scientific studies in various fields.
I will then present some software engineering and AI techniques that can support the strategic exploration of variability spaces. These include the use of abstractions and models (e.g., feature models), sampling strategies (e.g., uniform, random), cost-effective measurements (e.g., incremental build of software configurations), and dimensionality reduction methods (e.g., transfer learning, feature selection, software debloating).
I will finally argue that deep variability is both the problem and solution of frictionless reproducibility, calling the software science community to develop new methods and tools to manage variability and foster reproducibility in software systems.
Exposé invité Journées Nationales du GDR GPL 2024
8.Isolation of pure cultures and preservation of cultures.pdf
Isolation of pure culture, its various method.
Applied Science: Thermodynamics, Laws & Methodology.pdf
When I was asked to give a companion lecture in support of ‘The Philosophy of Science’ (https://shorturl.at/4pUXz) I decided not to walk through the detail of the many methodologies in order of use. Instead, I chose to employ a long standing, and ongoing, scientific development as an exemplar. And so, I chose the ever evolving story of Thermodynamics as a scientific investigation at its best.
Conducted over a period of >200 years, Thermodynamics R&D, and application, benefitted from the highest levels of professionalism, collaboration, and technical thoroughness. New layers of application, methodology, and practice were made possible by the progressive advance of technology. In turn, this has seen measurement and modelling accuracy continually improved at a micro and macro level.
Perhaps most importantly, Thermodynamics rapidly became a primary tool in the advance of applied science/engineering/technology, spanning micro-tech, to aerospace and cosmology. I can think of no better a story to illustrate the breadth of scientific methodologies and applications at their best.
Nucleic Acid-its structural and functional complexity.
This presentation explores a brief idea about the structural and functional attributes of nucleotides, the structure and function of genetic materials along with the impact of UV rays and pH upon them.
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/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.
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.
Cytokines and their role in immune regulation.pptx
This presentation covers the content and information on "Cytokines " and their role in immune regulation .
Shallowest Oil Discovery of Turkiye.pptx
The Petroleum System of the Çukurova Field - the Shallowest Oil Discovery of Türkiye, Adana
What is greenhouse gasses and how many gasses are there to affect the Earth.
What are greenhouse gasses how they affect the earth and its environment what is the future of the environment and earth how the weather and the climate effects.
ESR spectroscopy in liquid food and beverages.pptx
With increasing population, people need to rely on packaged food stuffs. Packaging of food materials requires the preservation of food. There are various methods for the treatment of food to preserve them and irradiation treatment of food is one of them. It is the most common and the most harmless method for the food preservation as it does not alter the necessary micronutrients of food materials. Although irradiated food doesn’t cause any harm to the human health but still the quality assessment of food is required to provide consumers with necessary information about the food. ESR spectroscopy is the most sophisticated way to investigate the quality of the food and the free radicals induced during the processing of the food. ESR spin trapping technique is useful for the detection of highly unstable radicals in the food. The antioxidant capability of liquid food and beverages in mainly performed by spin trapping technique.
原版制作(carleton毕业证书)卡尔顿大学毕业证硕士文凭原版一模一样
原版纸张【微信：741003700 】【(carleton毕业证书)卡尔顿大学毕业证】【微信：741003700 】学位证，留信认证（真实可查，永久存档）offer、雅思、外壳等材料/诚信可靠,可直接看成品样本，帮您解决无法毕业带来的各种难题！外壳，原版制作，诚信可靠，可直接看成品样本。行业标杆！精益求精，诚心合作，真诚制作！多年品质 ,按需精细制作，24小时接单,全套进口原装设备。十五年致力于帮助留学生解决难题，包您满意。
本公司拥有海外各大学样板无数，能完美还原海外各大学 Bachelor Diploma degree, Master Degree Diploma
1:1完美还原海外各大学毕业材料上的工艺：水印，阴影底纹，钢印LOGO烫金烫银，LOGO烫金烫银复合重叠。文字图案浮雕、激光镭射、紫外荧光、温感、复印防伪等防伪工艺。材料咨询办理、认证咨询办理请加学历顾问Q/微741003700
留信网认证的作用:
1:该专业认证可证明留学生真实身份
2:同时对留学生所学专业登记给予评定
3:国家专业人才认证中心颁发入库证书
4:这个认证书并且可以归档倒地方
5:凡事获得留信网入网的信息将会逐步更新到个人身份内，将在公安局网内查询个人身份证信息后，同步读取人才网入库信息
6:个人职称评审加20分
7:个人信誉贷款加10分
8:在国家人才网主办的国家网络招聘大会中纳入资料，供国家高端企业选择人才
ANAMOLOUS SECONDARY GROWTH IN DICOT ROOTS.pptx
Abnormal or anomalous secondary growth in plants. It defines secondary growth as an increase in plant girth due to vascular cambium or cork cambium. Anomalous secondary growth does not follow the normal pattern of a single vascular cambium producing xylem internally and phloem externally.
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
Nucleophilic Addition of carbonyl compounds.pptx
Nucleophilic addition is the most important reaction of carbonyls. Not just aldehydes and ketones, but also carboxylic acid derivatives in general.
Carbonyls undergo addition reactions with a large range of nucleophiles.
Comparing the relative basicity of the nucleophile and the product is extremely helpful in determining how reversible the addition reaction is. Reactions with Grignards and hydrides are irreversible. Reactions with weak bases like halides and carboxylates generally don’t happen.
Electronic effects (inductive effects, electron donation) have a large impact on reactivity.
Large groups adjacent to the carbonyl will slow the rate of reaction.
Neutral nucleophiles can also add to carbonyls, although their additions are generally slower and more reversible. Acid catalysis is sometimes employed to increase the rate of addition.
Recently uploaded (20)
Deep Software Variability and Frictionless Reproducibility
Deep Software Variability and Frictionless Reproducibility
8.Isolation of pure cultures and preservation of cultures.pdf
8.Isolation of pure cultures and preservation of cultures.pdf
Applied Science: Thermodynamics, Laws & Methodology.pdf
Applied Science: Thermodynamics, Laws & Methodology.pdf
Nucleic Acid-its structural and functional complexity.
Nucleic Acid-its structural and functional complexity.
Remote Sensing and Computational, Evolutionary, Supercomputing, and Intellige...
Remote Sensing and Computational, Evolutionary, Supercomputing, and Intellige...
The debris of the ‘last major merger’ is dynamically young
The debris of the ‘last major merger’ is dynamically young
Unlocking the mysteries of reproduction: Exploring fecundity and gonadosomati...
Unlocking the mysteries of reproduction: Exploring fecundity and gonadosomati...
Cytokines and their role in immune regulation.pptx
Cytokines and their role in immune regulation.pptx
What is greenhouse gasses and how many gasses are there to affect the Earth.
What is greenhouse gasses and how many gasses are there to affect the Earth.
ESR spectroscopy in liquid food and beverages.pptx
ESR spectroscopy in liquid food and beverages.pptx
aziz sancar nobel prize winner: from mardin to nobel
aziz sancar nobel prize winner: from mardin to nobel
Equivariant neural networks and representation theory
Equivariant neural networks and representation theory
Protein structure levels
- 1. Four Levels of Protein Structure
- 2. Four Levels of Protein Structure • Primary Structure: Linear Sequence of Amino Acids C CH2N H R Each amino acid hasEach amino acid has central carbon liked tocentral carbon liked to ---hydrogen (H)---hydrogen (H) ---amino group (NH---amino group (NH22)) ---acid group (COOH)---acid group (COOH) ---unique group (R)---unique group (R) O OH
- 4. The carboxyl group of one amino acid is linkedThe carboxyl group of one amino acid is linked to the amino group of the next amino acid.to the amino group of the next amino acid.
- 5. Four Levels of Protein Structure • Primary Structure: Amino Acids are linked with a covalent bond called a peptide bond. C CH2N H R1 O N C C O OH H R2 H
- 6. Four Levels of Protein Structure • Secondary Structure: Folded structure due to hydrogen bonds between the amino and acid groups of amino acids C O N H C O N H C O N H C O N H or
- 7. Four Levels of Protein Structure • Tertiary Structure: Three dimensional folded structure due to attractions and repulsions between R groups All but peptide bonds areAll but peptide bonds are involved in tertiary structure.involved in tertiary structure.
- 9. Four Levels of Protein Structure • Quaternary structure: Association of two or more protein chains eg. Hemoglobin is composed ofeg. Hemoglobin is composed of 4 protein chains4 protein chains 2 are called alpha hemoglobin2 are called alpha hemoglobin 2 are called beta hemoglobin2 are called beta hemoglobin
- 10. Applying Your Knowledge A. Which structure results exclusively from hydrogen bonding? B. Which structure involves an association of two or more protein chains? C. Which structure describes the linear sequence of amino acids? D. Which structure depends upon interactions between the R groups of the amino acids? 1. Primary 2. Secondary 3. Tertiary 4. Quaternary