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.
This document discusses the structure and functions of proteins. It explains that proteins have primary, secondary, tertiary, and quaternary levels of structure which determine their function. Fibrous proteins have structural functions like collagen, while globular proteins have metabolic functions like hemoglobin. The primary structure is the sequence of amino acids in the polypeptide chain. Secondary and tertiary structures form due to bonding which creates the 3D shape of the protein, important for its specific function of interacting with other molecules.
The document discusses the structure and function of cell components. It notes that living systems are composed of carbon, hydrogen, oxygen, nitrogen, phosphorus, and sulfur. The carbon atom forms complex biologically important molecules through covalent bonds. Many polymers in cells are composed of monomers linked by dehydration reactions, which can be reversed by hydrolysis reactions. These polymerization and depolymerization reactions are important in cell metabolism and require energy to synthesize complex structures in anabolic or biosynthetic reactions.
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 have many important functions in the body including structure, catalysis, movement, transport, hormones, protection, storage, and regulation. They are composed of amino acids that are linked together through peptide bonds to form polypeptide chains or folded structures. The structure of proteins includes primary, secondary, tertiary, and sometimes quaternary levels that determine the protein's shape and function. Denaturation can disrupt a protein's structure through physical or chemical means.
This document provides an introduction and overview of protein structure and classification. It discusses the basic building blocks of proteins, the four levels of protein structure (primary, secondary, tertiary, and quaternary), and two main methods of protein classification - by shape (globular vs. fibrous proteins) and by function (enzymes, hormones, structural proteins, etc.). The document aims to cover key concepts about protein structure and organization in a comprehensive yet concise manner.
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.
This document discusses the primary, secondary, tertiary, and quaternary structure of proteins. It begins by describing the important biological functions of proteins and the general structures of globular and fibrous proteins. It then discusses the structures of amino acids and how peptide bonds link amino acids into polypeptide chains. The levels of protein structure are introduced, including the alpha helix and beta sheet secondary structures, tertiary folding of polypeptide chains, and arrangement of subunits in quaternary structure. Common protein domains and motifs are also illustrated.
Proteins 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.
This document discusses the structure and functions of proteins. It explains that proteins have primary, secondary, tertiary, and quaternary levels of structure which determine their function. Fibrous proteins have structural functions like collagen, while globular proteins have metabolic functions like hemoglobin. The primary structure is the sequence of amino acids in the polypeptide chain. Secondary and tertiary structures form due to bonding which creates the 3D shape of the protein, important for its specific function of interacting with other molecules.
The document discusses the structure and function of cell components. It notes that living systems are composed of carbon, hydrogen, oxygen, nitrogen, phosphorus, and sulfur. The carbon atom forms complex biologically important molecules through covalent bonds. Many polymers in cells are composed of monomers linked by dehydration reactions, which can be reversed by hydrolysis reactions. These polymerization and depolymerization reactions are important in cell metabolism and require energy to synthesize complex structures in anabolic or biosynthetic reactions.
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 have many important functions in the body including structure, catalysis, movement, transport, hormones, protection, storage, and regulation. They are composed of amino acids that are linked together through peptide bonds to form polypeptide chains or folded structures. The structure of proteins includes primary, secondary, tertiary, and sometimes quaternary levels that determine the protein's shape and function. Denaturation can disrupt a protein's structure through physical or chemical means.
This document provides an introduction and overview of protein structure and classification. It discusses the basic building blocks of proteins, the four levels of protein structure (primary, secondary, tertiary, and quaternary), and two main methods of protein classification - by shape (globular vs. fibrous proteins) and by function (enzymes, hormones, structural proteins, etc.). The document aims to cover key concepts about protein structure and organization in a comprehensive yet concise manner.
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.
This document discusses the primary, secondary, tertiary, and quaternary structure of proteins. It begins by describing the important biological functions of proteins and the general structures of globular and fibrous proteins. It then discusses the structures of amino acids and how peptide bonds link amino acids into polypeptide chains. The levels of protein structure are introduced, including the alpha helix and beta sheet secondary structures, tertiary folding of polypeptide chains, and arrangement of subunits in quaternary structure. Common protein domains and motifs are also illustrated.
Proteins by Salman Saeed Lecturer Botany UCMS KhanewalSalman Saeed
This document discusses proteins and their structure and function. It begins by introducing proteins as polymers made of amino acids linked into peptide chains. It then covers the 20 main amino acids, how they are classified, and how peptide bonds form. It describes the primary, secondary, tertiary, and quaternary structural organization of proteins. Specific proteins discussed include hemoglobin, which transports oxygen in our blood, and myoglobin, which stores oxygen in muscles.
Amino acids of biological importance 2021Ayman Hany
This document discusses amino acids and proteins of biological importance. It defines amino acids as organic acids that contain one or more amino groups. Proteins are formed from chains of 50 or more amino acids linked by peptide bonds. The document classifies amino acids and discusses the structures of proteins including primary, secondary, tertiary and quaternary structure. It also addresses the denaturation and conformational classification of 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.
This document discusses the structure of proteins at multiple levels:
1. It describes the primary structure of proteins as the unique sequence of amino acids determined by genes. The peptide bond links amino acids and is rigid and planar.
2. Secondary structures like alpha helices and beta sheets form due to hydrogen bonding between amino acids in close proximity in the sequence. Alpha helices are tightly coiled and stabilized by hydrogen bonds between amino and carbonyl groups.
3. Tertiary structure refers to the compact three-dimensional folding of the protein chain, bringing hydrophobic residues inwards and hydrophilic outwards. Disulfide bonds and other interactions contribute to tertiary structure.
4. Some proteins have quaternary structure
Proteins are made up of chains of amino acids that fold into complex three-dimensional shapes determined by their primary, secondary, and tertiary structures. The primary structure is the linear sequence of amino acids in the polypeptide chain. Secondary structures form due to hydrogen bonding and include alpha helices and beta sheets. Tertiary structure describes the overall folded shape of the protein determined by interactions between amino acid side chains.
Proteins are made up of elements like carbon, hydrogen, oxygen, nitrogen, sulfur, and phosphorus. They are formed through condensation reactions between amino acids and can be broken down through hydrolysis. 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 alpha helices and beta sheets, tertiary is the overall 3D shape, and quaternary involves combinations of tertiary structures. There are essential and non-essential amino acids, with essential ones not synthesized by the body.
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.
Proteins are large molecules composed of chains of amino acids. There are 20 types of amino acids that combine to form proteins. Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. They perform many critical functions in the body according to their shape, which can be altered through denaturing.
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.
Tertiary structure describes how protein chains fold upon themselves into complex 3D shapes. These shapes are stabilized by interactions between amino acid side chains like disulfide bonds, hydrogen bonds, and hydrophobic interactions. Long protein chains often contain multiple domains that fold independently. Quaternary structure refers to complexes of two or more protein subunits. Chaperone proteins assist other proteins in proper folding, while misfolded proteins can accumulate and cause diseases.
The document discusses the four levels of protein structure - primary, secondary, tertiary, and quaternary. It explains the significance of each level. The primary structure is the sequence of amino acids. The secondary structure involves hydrogen bonding that forms alpha helices and beta sheets. Tertiary structure describes the overall 3D shape formed by interactions between secondary structures. Quaternary structure refers to complexes of multiple polypeptide chains. The document also discusses membrane proteins and the roles of polar and non-polar amino acids in protein structure and function.
8. amino acids and proteins structures and chemistry Happy Learning
Amino acids are the building blocks of proteins. They contain both amino and carboxyl groups and come in L- and D-forms based on their chirality. There are 20 standard amino acids which are classified by the properties of their R-groups. Amino acids join together via peptide bonds to form polypeptide chains. Proteins attain their structure through four levels - primary, secondary, tertiary, and quaternary. Secondary structures include alpha helices and beta sheets formed by hydrogen bonding. Tertiary structure describes the 3D folding of a single polypeptide chain. Quaternary structure involves interactions between multiple polypeptide subunits.
The document discusses the four levels of structural organization of proteins: primary, secondary, tertiary, and quaternary structure. It describes the primary structure as the linear sequence of amino acids in a protein. Secondary structures form due to hydrogen bonding and include alpha helices and beta sheets. Tertiary structure refers to the three dimensional folding of a protein chain. Quaternary structure occurs when multiple protein chains combine to form a functional protein. The document focuses on different types of secondary structures like alpha helices, beta sheets, loops, and turns.
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.
The document discusses the levels of protein structure from primary to quaternary structure. It defines the primary structure as the amino acid sequence. Secondary structure forms from hydrogen bonding between amino acids and includes alpha helices and beta pleated sheets. Tertiary structure results from folding influenced by interactions between amino acid side chains. Quaternary structure occurs when multiple polypeptide chains interact to form a protein complex. Examples including hemoglobin and glyceraldehyde-3-phosphate dehydrogenase are provided to illustrate the different levels of structure.
The document discusses protein structure and function. It begins by introducing proteins as linear polymers made of amino acids, with the sequence specified by DNA. It then describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. Primary structure refers to the sequence of amino acids. Secondary structure involves regular conformations like coils and folds. Tertiary structure describes the 3D shape of the whole protein chain. Quaternary structure involves interactions between multiple protein subunits in a complex. The document also lists the 20 common amino acids and provides references for further reading.
Transamidation of available glutamine residues is catalyzed by trans-
glutaminases (TGs) through a calcium-dependent acyl transfer reac-
tion.
Proteins are posttranslationally modified by an acyl transfer
reaction between the g- carboxamide group of glutamine residues
And the e-amino group of peptide-bound lysine residues
or the primary amino group of polyamines to form either e-(g-
glutamy l)lysine or (g- glutamyl )polyamine bonds between proteins,
releasing ammonia.
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 bonds. Tertiary structure is the three-dimensional folding determined by interactions between secondary structures. Quaternary structure involves interactions between multiple polypeptide chains. Proteins can also be classified based on shape, function, and composition. Denaturation disrupts non-covalent bonds leading to loss of native structure and biological function.
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.
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.
Proteins by Salman Saeed Lecturer Botany UCMS KhanewalSalman Saeed
This document discusses proteins and their structure and function. It begins by introducing proteins as polymers made of amino acids linked into peptide chains. It then covers the 20 main amino acids, how they are classified, and how peptide bonds form. It describes the primary, secondary, tertiary, and quaternary structural organization of proteins. Specific proteins discussed include hemoglobin, which transports oxygen in our blood, and myoglobin, which stores oxygen in muscles.
Amino acids of biological importance 2021Ayman Hany
This document discusses amino acids and proteins of biological importance. It defines amino acids as organic acids that contain one or more amino groups. Proteins are formed from chains of 50 or more amino acids linked by peptide bonds. The document classifies amino acids and discusses the structures of proteins including primary, secondary, tertiary and quaternary structure. It also addresses the denaturation and conformational classification of 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.
This document discusses the structure of proteins at multiple levels:
1. It describes the primary structure of proteins as the unique sequence of amino acids determined by genes. The peptide bond links amino acids and is rigid and planar.
2. Secondary structures like alpha helices and beta sheets form due to hydrogen bonding between amino acids in close proximity in the sequence. Alpha helices are tightly coiled and stabilized by hydrogen bonds between amino and carbonyl groups.
3. Tertiary structure refers to the compact three-dimensional folding of the protein chain, bringing hydrophobic residues inwards and hydrophilic outwards. Disulfide bonds and other interactions contribute to tertiary structure.
4. Some proteins have quaternary structure
Proteins are made up of chains of amino acids that fold into complex three-dimensional shapes determined by their primary, secondary, and tertiary structures. The primary structure is the linear sequence of amino acids in the polypeptide chain. Secondary structures form due to hydrogen bonding and include alpha helices and beta sheets. Tertiary structure describes the overall folded shape of the protein determined by interactions between amino acid side chains.
Proteins are made up of elements like carbon, hydrogen, oxygen, nitrogen, sulfur, and phosphorus. They are formed through condensation reactions between amino acids and can be broken down through hydrolysis. 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 alpha helices and beta sheets, tertiary is the overall 3D shape, and quaternary involves combinations of tertiary structures. There are essential and non-essential amino acids, with essential ones not synthesized by the body.
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.
Proteins are large molecules composed of chains of amino acids. There are 20 types of amino acids that combine to form proteins. Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. They perform many critical functions in the body according to their shape, which can be altered through denaturing.
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.
Tertiary structure describes how protein chains fold upon themselves into complex 3D shapes. These shapes are stabilized by interactions between amino acid side chains like disulfide bonds, hydrogen bonds, and hydrophobic interactions. Long protein chains often contain multiple domains that fold independently. Quaternary structure refers to complexes of two or more protein subunits. Chaperone proteins assist other proteins in proper folding, while misfolded proteins can accumulate and cause diseases.
The document discusses the four levels of protein structure - primary, secondary, tertiary, and quaternary. It explains the significance of each level. The primary structure is the sequence of amino acids. The secondary structure involves hydrogen bonding that forms alpha helices and beta sheets. Tertiary structure describes the overall 3D shape formed by interactions between secondary structures. Quaternary structure refers to complexes of multiple polypeptide chains. The document also discusses membrane proteins and the roles of polar and non-polar amino acids in protein structure and function.
8. amino acids and proteins structures and chemistry Happy Learning
Amino acids are the building blocks of proteins. They contain both amino and carboxyl groups and come in L- and D-forms based on their chirality. There are 20 standard amino acids which are classified by the properties of their R-groups. Amino acids join together via peptide bonds to form polypeptide chains. Proteins attain their structure through four levels - primary, secondary, tertiary, and quaternary. Secondary structures include alpha helices and beta sheets formed by hydrogen bonding. Tertiary structure describes the 3D folding of a single polypeptide chain. Quaternary structure involves interactions between multiple polypeptide subunits.
The document discusses the four levels of structural organization of proteins: primary, secondary, tertiary, and quaternary structure. It describes the primary structure as the linear sequence of amino acids in a protein. Secondary structures form due to hydrogen bonding and include alpha helices and beta sheets. Tertiary structure refers to the three dimensional folding of a protein chain. Quaternary structure occurs when multiple protein chains combine to form a functional protein. The document focuses on different types of secondary structures like alpha helices, beta sheets, loops, and turns.
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.
The document discusses the levels of protein structure from primary to quaternary structure. It defines the primary structure as the amino acid sequence. Secondary structure forms from hydrogen bonding between amino acids and includes alpha helices and beta pleated sheets. Tertiary structure results from folding influenced by interactions between amino acid side chains. Quaternary structure occurs when multiple polypeptide chains interact to form a protein complex. Examples including hemoglobin and glyceraldehyde-3-phosphate dehydrogenase are provided to illustrate the different levels of structure.
The document discusses protein structure and function. It begins by introducing proteins as linear polymers made of amino acids, with the sequence specified by DNA. It then describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. Primary structure refers to the sequence of amino acids. Secondary structure involves regular conformations like coils and folds. Tertiary structure describes the 3D shape of the whole protein chain. Quaternary structure involves interactions between multiple protein subunits in a complex. The document also lists the 20 common amino acids and provides references for further reading.
Transamidation of available glutamine residues is catalyzed by trans-
glutaminases (TGs) through a calcium-dependent acyl transfer reac-
tion.
Proteins are posttranslationally modified by an acyl transfer
reaction between the g- carboxamide group of glutamine residues
And the e-amino group of peptide-bound lysine residues
or the primary amino group of polyamines to form either e-(g-
glutamy l)lysine or (g- glutamyl )polyamine bonds between proteins,
releasing ammonia.
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 bonds. Tertiary structure is the three-dimensional folding determined by interactions between secondary structures. Quaternary structure involves interactions between multiple polypeptide chains. Proteins can also be classified based on shape, function, and composition. Denaturation disrupts non-covalent bonds leading to loss of native structure and biological function.
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.
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.
Proteins are the macromolecules responsible for the biological processes in the cell. They consist at their most basic level of a chain of amino acids, determined by the sequence of nucleotides in a gene. Depending on the amino acid sequence (different amino acids have different biochemical properties) and interactions with their environment, proteins fold into a three-dimensional structure, which allows them to interact with other proteins and molecules and perform their function
The document discusses protein structure at multiple levels of organization. It describes the 20 amino acids that make up proteins and how they can be categorized based on properties like size and affinity for water. It then explains how amino acids join together through peptide bonds to form the primary structure of a protein as a linear sequence. Secondary structures like alpha helices and beta sheets involve hydrogen bonding between amino acids to create regular local structures. Tertiary structure refers to the overall 3D shape formed by packing and arrangement of secondary structures. There are two main types of tertiary structure - globular proteins that are soluble and membrane proteins that exist in cell membranes.
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.
- 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
Folding depends upon sequence of Amino Acids not the Composition. Folding starts with the secondary structure and ends at quaternary structure.
Denaturation occur at secondary, tertiary & quaternary level but not at primary level.
Protein Folding-biophysical and cellular aspects, protein denaturationAnishaMukherjee5
Protein folding is the physical process by which a protein chain acquires its native 3-dimensional structure, a conformation that is usually biologically functional, in an expeditious and reproducible manner.
Proteins-Classification ,Structure of protein, properties and biological impo...SoniaBajaj10
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.
Proteins are linear polymers of amino acids linked by peptide bonds. There are 20 different amino acids that make up proteins. Proteins have four levels of structure - primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids, secondary structure involves folding into shapes like alpha helices and beta sheets, tertiary structure is the overall 3D shape of the protein, and quaternary structure involves the joining of multiple protein subunits. Proteins play many important roles in the body such as enzymes, transport, structure, and regulation.
Proteins are polymers of amino acids that form unique 3D structures essential for cellular structure and function. They are composed of amino acid building blocks that vary in polarity and allow proteins to fold into complex shapes defined by their primary, secondary, tertiary, and quaternary structure levels. Protein structure enables a diverse range of functions including catalysis, transport, structure, and movement.
Collagen and elastin are fibrous proteins that provide structure in the body. Collagen forms a rigid triple helix structure made of three polypeptide chains. It is abundant in skin, bone, and cartilage. Elastin provides elasticity and is found in lungs, arteries, and ligaments. Both proteins derive their mechanical properties from their unique secondary and tertiary structures, which are stabilized by interactions between amino acid side chains.
Collagen and elastin are fibrous proteins that provide structure in the body. Collagen forms a rigid triple helix structure made of three polypeptide chains. It is abundant in skin, bone, and cartilage. Elastin provides elasticity and is found in lungs, arteries, and ligaments. Both proteins derive their mechanical properties from their unique secondary and tertiary structures, which are stabilized by interactions between amino acid side chains.
This document discusses protein structure and folding. It describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structure involves folding into alpha helices or beta sheets. Tertiary structure is the overall 3D shape formed by interactions between amino acid side chains. Quaternary structure refers to interactions between multiple polypeptide chains in a protein. The document also discusses protein folding, denaturation, and misfolding, noting that many neurodegenerative diseases are associated with misfolded protein aggregates.
9.amino acids and proteins structures and chemistry Happy Learning
1. Amino acids are organic compounds with amino and carboxyl groups that are the building blocks of proteins. They exist in L- and D-stereoisomers and can be classified based on their variable R groups.
2. Proteins have primary, secondary, tertiary, and quaternary levels of structure. The primary structure is the amino acid sequence, and secondary structures include alpha helices and beta sheets formed by hydrogen bonding. Tertiary structure describes the folding of the polypeptide chain, and quaternary when multiple polypeptide chains assemble.
3. Mutations affecting collagen, alpha-1-antitrypsin, hemoglobin, and other proteins can lead to diseases like
Sexuality - Issues, Attitude and Behaviour - Applied Social Psychology - Psyc...PsychoTech Services
A proprietary approach developed by bringing together the best of learning theories from Psychology, design principles from the world of visualization, and pedagogical methods from over a decade of training experience, that enables you to: Learn better, faster!
Mechanisms and Applications of Antiviral Neutralizing Antibodies - Creative B...Creative-Biolabs
Neutralizing antibodies, pivotal in immune defense, specifically bind and inhibit viral pathogens, thereby playing a crucial role in protecting against and mitigating infectious diseases. In this slide, we will introduce what antibodies and neutralizing antibodies are, the production and regulation of neutralizing antibodies, their mechanisms of action, classification and applications, as well as the challenges they face.
Evidence of Jet Activity from the Secondary Black Hole in the OJ 287 Binary S...Sérgio Sacani
Wereport the study of a huge optical intraday flare on 2021 November 12 at 2 a.m. UT in the blazar OJ287. In the binary black hole model, it is associated with an impact of the secondary black hole on the accretion disk of the primary. Our multifrequency observing campaign was set up to search for such a signature of the impact based on a prediction made 8 yr earlier. The first I-band results of the flare have already been reported by Kishore et al. (2024). Here we combine these data with our monitoring in the R-band. There is a big change in the R–I spectral index by 1.0 ±0.1 between the normal background and the flare, suggesting a new component of radiation. The polarization variation during the rise of the flare suggests the same. The limits on the source size place it most reasonably in the jet of the secondary BH. We then ask why we have not seen this phenomenon before. We show that OJ287 was never before observed with sufficient sensitivity on the night when the flare should have happened according to the binary model. We also study the probability that this flare is just an oversized example of intraday variability using the Krakow data set of intense monitoring between 2015 and 2023. We find that the occurrence of a flare of this size and rapidity is unlikely. In machine-readable Tables 1 and 2, we give the full orbit-linked historical light curve of OJ287 as well as the dense monitoring sample of Krakow.
Mending Clothing to Support Sustainable Fashion_CIMaR 2024.pdfSelcen Ozturkcan
Ozturkcan, S., Berndt, A., & Angelakis, A. (2024). Mending clothing to support sustainable fashion. Presented at the 31st Annual Conference by the Consortium for International Marketing Research (CIMaR), 10-13 Jun 2024, University of Gävle, Sweden.
Microbial interaction
Microorganisms interacts with each other and can be physically associated with another organisms in a variety of ways.
One organism can be located on the surface of another organism as an ectobiont or located within another organism as endobiont.
Microbial interaction may be positive such as mutualism, proto-cooperation, commensalism or may be negative such as parasitism, predation or competition
Types of microbial interaction
Positive interaction: mutualism, proto-cooperation, commensalism
Negative interaction: Ammensalism (antagonism), parasitism, predation, competition
I. Mutualism:
It is defined as the relationship in which each organism in interaction gets benefits from association. It is an obligatory relationship in which mutualist and host are metabolically dependent on each other.
Mutualistic relationship is very specific where one member of association cannot be replaced by another species.
Mutualism require close physical contact between interacting organisms.
Relationship of mutualism allows organisms to exist in habitat that could not occupied by either species alone.
Mutualistic relationship between organisms allows them to act as a single organism.
Examples of mutualism:
i. Lichens:
Lichens are excellent example of mutualism.
They are the association of specific fungi and certain genus of algae. In lichen, fungal partner is called mycobiont and algal partner is called
II. Syntrophism:
It is an association in which the growth of one organism either depends on or improved by the substrate provided by another organism.
In syntrophism both organism in association gets benefits.
Compound A
Utilized by population 1
Compound B
Utilized by population 2
Compound C
utilized by both Population 1+2
Products
In this theoretical example of syntrophism, population 1 is able to utilize and metabolize compound A, forming compound B but cannot metabolize beyond compound B without co-operation of population 2. Population 2is unable to utilize compound A but it can metabolize compound B forming compound C. Then both population 1 and 2 are able to carry out metabolic reaction which leads to formation of end product that neither population could produce alone.
Examples of syntrophism:
i. Methanogenic ecosystem in sludge digester
Methane produced by methanogenic bacteria depends upon interspecies hydrogen transfer by other fermentative bacteria.
Anaerobic fermentative bacteria generate CO2 and H2 utilizing carbohydrates which is then utilized by methanogenic bacteria (Methanobacter) to produce methane.
ii. Lactobacillus arobinosus and Enterococcus faecalis:
In the minimal media, Lactobacillus arobinosus and Enterococcus faecalis are able to grow together but not alone.
The synergistic relationship between E. faecalis and L. arobinosus occurs in which E. faecalis require folic acid
JAMES WEBB STUDY THE MASSIVE BLACK HOLE SEEDSSérgio Sacani
The pathway(s) to seeding the massive black holes (MBHs) that exist at the heart of galaxies in the present and distant Universe remains an unsolved problem. Here we categorise, describe and quantitatively discuss the formation pathways of both light and heavy seeds. We emphasise that the most recent computational models suggest that rather than a bimodal-like mass spectrum between light and heavy seeds with light at one end and heavy at the other that instead a continuum exists. Light seeds being more ubiquitous and the heavier seeds becoming less and less abundant due the rarer environmental conditions required for their formation. We therefore examine the different mechanisms that give rise to different seed mass spectrums. We show how and why the mechanisms that produce the heaviest seeds are also among the rarest events in the Universe and are hence extremely unlikely to be the seeds for the vast majority of the MBH population. We quantify, within the limits of the current large uncertainties in the seeding processes, the expected number densities of the seed mass spectrum. We argue that light seeds must be at least 103 to 105 times more numerous than heavy seeds to explain the MBH population as a whole. Based on our current understanding of the seed population this makes heavy seeds (Mseed > 103 M⊙) a significantly more likely pathway given that heavy seeds have an abundance pattern than is close to and likely in excess of 10−4 compared to light seeds. Finally, we examine the current state-of-the-art in numerical calculations and recent observations and plot a path forward for near-future advances in both domains.
2. INTRODUCTION
Proteins are important class of biological
macromolecules which are the polymer of amino acid
There are several levels of structural organisation of
proteins . They are :-
i. Primary structure
ii. Secondary structure
iii. Tertiary structure
iv. Quarternery structure
6. PRIMARY STRUCTURE
The primary structure
of protein refers to the
sequence of amino acid
present in a
polypeptide chain
Amino acid are
covalently linked by
peptide bond
Peptide bond is
formed by the removal
of one water molecule .
The 10 structure of
protein start from the
amino terminal (N) end
7. To predict the 2o and 30
structure from sequence
homologies with related
protein .
Many genetic disease arise
from abnormal amino
acid sequence
To understand the
molecular mechanism of
action of protein
To find the evolutionary
path
Gene sequencing method .
Edman degradation - the
amino terminal residue is
labeled and cleaved from
the peptide without
disrupting the peptide
bonds between other
amino acid residues.
IMPORTANCE OF PRIMARY
STRUCTURE
METHOD OF AA
SEQUENCE
DETERMINATION
8. SECONDARY STRUCTURE
Localized arragement of adjacent AA formed as the polypeptide
chain folds
Alpha helices are the most common form of secondary structure
formed by the right hand coiling of the primary structure of the
protein
Coiling is caused by the H bond interaction between the AA of
the protein
Secondary structure consist of :-
a Helix
b pleated sheet
b bends
Super secondary structure
9.
10.
11.
12.
13. BETA BENDS
Permits the change of the
direction of the peptide
chain to get a folded
structure
It gives protein globularity
rather than linearity
H bond stablizes the beta
turn structure
Proline and glycine are
frequently found in beta
turns
Beta turns often promote
the formation of
antiparallel beta sheets
14. SUPER SECONDARY STRUCTURE
Present in Globular
protein
This structure form
when two b pleated
sheath are connected
to each other by an
alpha helix
Example :- b-a-b
supersecondary motif
15. TERTIARY STRUCTURE
Tertiary structure is the
three dimensional
conformation of a
polypeptide .
The common features of
protein tertiary structure
reveal much about the
biological functions of the
proteins and their
evolutionary origins
The function of a protein
depends upon on its
tertiary structure if this is
disrupted, it loses its
activity .
16. INTERACTIONS STABILIZING 30
STRUCTURE
The final shape is
determined by variety
of bonding interaction
between the side chain
of the amino acid
• Hydrogen bond
• Ionic bond
• Disulphide bridges
• Hydrophobic
Interactions
17. DETERMINATION OF THE TERTIARY
STRUCTURE
The protein structure can be studied through :-
• X- ray crystallographic studies
• Nuclear magnetic resonance
Most of the structure is deposited in a database
known as protein database bank (PDB) ,it allows the
tertiary structure of variety of proteins to be
analyzed and compared
18. QUATERNARY STRUCTURE
Biological function of
some molecules is
determined by multiple
polypeptide chains –
multimeric proteins
Arrangment of
polypeptide sub unit is
called as quaternary
structure
Sub unit are held together
by non covalent
interactions
Eg - Heamoglobin (a2b2)
19. CLASSIFICATION BASED ON SHAPE
Depending upon the axial ratio protein has been
classified into two types :-
I. Fibrous protein
II. Globular protein
20. FIBROUS PROTEIN
Axial ratio more than 10
Long thread like molecule
Their helical strand mainly forms fibres
These protein are insoluble in water
Form structure of the tissue
Present where support is required
Example :- collagen , elastin , keratin
21. GLOBULAR PROTEIN
Axial ratio less than 10
Spheroid or ovoid in shape
Enzymes are mostly globular in shape
Subdivide into two types of protein :-
I. Albumin : soluble in water
II. Globulin : soluble in dilute salt solution
22. CLASSIFICATION BASED ON FUNCTION
Catalytic protein :- These are the enzyme which may be simple
or conjugated
I. Alkaline phosphotase
II. Alanine Transaminase
Regulatory or Hormonal protein :- Many protein acts as
hormone
I. Insulin
II. Growth Hormone
Structural protein :- Contribute to the structure of tissue
I. Collagen
II. Elastin
23. Transport protein :- Serve to carry substances
I. Transferrin carry iron
II. Heamoglobin carry oxygen
Immune protein :- Serve in the defence mechanism
I. Immunoglobulin - IgA , IgG , IgM , IgE , IgD
Contractile protein :- Takes part in muscle
contraction
I. Actin
II. Myosin
24. Genetic protein :- Protein present in combination
with nucleic acid
I. Histone protein
Storage protein :- To store protein for nutritional
purpose
I. Casein in milk
II. Glaidin in wheat