This is my first Power point presentation of my university life.In this presentation Anyone Can get easy and clear information About Protein Classification & it's Features.
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
Proteins are complex organic molecules composed of amino acids linked by peptide bonds. They serve important structural and functional roles in the body. As the document outlines, proteins are classified based on their shape (globular or fibrous) or function, such as enzymes, hormones, structural proteins, transport proteins, and immune proteins. The four levels of protein structure - primary, secondary, tertiary, and quaternary - determine a protein's 3D structure. Proteins perform vital roles like muscle contraction, oxygen transport, preventing blood loss, and participating in metabolic reactions as enzymes. They are essential biomolecules that make up tissues and carry out important functions in the body.
Fibrous proteins are a group of proteins associated with rod or wire shapes. They are usually inert structural or storage proteins that are generally water insoluble. Examples include keratin, collagen, and elastin. In the early 1950s, the basic structures of fibrous proteins were determined to be long protein chains composed of amino acid strings that fold into limited structures like alpha helices and beta sheets. Fibrous proteins often have biological roles as structural components and are found in tissues like bone, cartilage, hair and skin.
• Description: In this video the viewers will come to know about different mode of classification of proteins. Proteins are classified based on their Solubility and composition, Function, Shape & size.
Portion explained:
Classification based on solubility and composition
Simple proteins
1. Albumins
2. Globulins
3. Prolamins
4. Glutelins
5. Histones
6. Protamines
7. Albuminoids
ii. Conjugated or compound proteins
1. Nucleoproteins
2. Mucoproteins
3. Chromoproteins
4. Lipoproteins
5. Metalloproteins
6. Phosphoproteins
B. Classification of proteins based on function
1. Catalytic proteins – Enzymes
2. Regulatory proteins – Hormones
3. Protective proteins – Antibodies
4. Storage proteins
5. Transport proteins
6. Toxic proteins
7. Structural proteins
8. Contractile proteins
9. Secretary proteins
10. Exotic proteins
C. Classification based on size and shape
Polysaccharide introduction, example, structure, starch, cellulose, chitin those structure and important functions and their presence in plants and animals, polysaccharide types based on functions and their composition , functions of polysaccharides , important images for relevant polysaccharides types, polysaccharide role in plants and animal cells. Starch - structure and functions, cellulose structure and functions, chitin - structure and functions
This document discusses the classification and structure of proteins. It describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. The secondary structure involves local folding patterns stabilized by hydrogen bonds. The tertiary structure is the overall three-dimensional shape of a protein determined by interactions between amino acid side chains. Quaternary structure refers to the arrangement of multiple protein subunits. The document also categorizes proteins based on their biological functions and physical properties.
This document discusses the classification and properties of proteins. It describes four levels of protein structure: primary, secondary, tertiary, and quaternary. Proteins can also be classified by their biological function, which includes enzymes, transport proteins, storage proteins, contractile/motile proteins, structural proteins, defense proteins, regulatory proteins, and other functional proteins. Classification by shape and solubility includes fibrous, globular, and membrane proteins. Classification by composition distinguishes between simple and conjugated proteins. Nutritionally, proteins are either complete or incomplete. The document concludes by discussing properties like denaturation and its causes like heat, alcohol, acids, bases, and heavy metal salts.
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
Proteins are complex organic molecules composed of amino acids linked by peptide bonds. They serve important structural and functional roles in the body. As the document outlines, proteins are classified based on their shape (globular or fibrous) or function, such as enzymes, hormones, structural proteins, transport proteins, and immune proteins. The four levels of protein structure - primary, secondary, tertiary, and quaternary - determine a protein's 3D structure. Proteins perform vital roles like muscle contraction, oxygen transport, preventing blood loss, and participating in metabolic reactions as enzymes. They are essential biomolecules that make up tissues and carry out important functions in the body.
Fibrous proteins are a group of proteins associated with rod or wire shapes. They are usually inert structural or storage proteins that are generally water insoluble. Examples include keratin, collagen, and elastin. In the early 1950s, the basic structures of fibrous proteins were determined to be long protein chains composed of amino acid strings that fold into limited structures like alpha helices and beta sheets. Fibrous proteins often have biological roles as structural components and are found in tissues like bone, cartilage, hair and skin.
• Description: In this video the viewers will come to know about different mode of classification of proteins. Proteins are classified based on their Solubility and composition, Function, Shape & size.
Portion explained:
Classification based on solubility and composition
Simple proteins
1. Albumins
2. Globulins
3. Prolamins
4. Glutelins
5. Histones
6. Protamines
7. Albuminoids
ii. Conjugated or compound proteins
1. Nucleoproteins
2. Mucoproteins
3. Chromoproteins
4. Lipoproteins
5. Metalloproteins
6. Phosphoproteins
B. Classification of proteins based on function
1. Catalytic proteins – Enzymes
2. Regulatory proteins – Hormones
3. Protective proteins – Antibodies
4. Storage proteins
5. Transport proteins
6. Toxic proteins
7. Structural proteins
8. Contractile proteins
9. Secretary proteins
10. Exotic proteins
C. Classification based on size and shape
Polysaccharide introduction, example, structure, starch, cellulose, chitin those structure and important functions and their presence in plants and animals, polysaccharide types based on functions and their composition , functions of polysaccharides , important images for relevant polysaccharides types, polysaccharide role in plants and animal cells. Starch - structure and functions, cellulose structure and functions, chitin - structure and functions
This document discusses the classification and structure of proteins. It describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. The secondary structure involves local folding patterns stabilized by hydrogen bonds. The tertiary structure is the overall three-dimensional shape of a protein determined by interactions between amino acid side chains. Quaternary structure refers to the arrangement of multiple protein subunits. The document also categorizes proteins based on their biological functions and physical properties.
This document discusses the classification and properties of proteins. It describes four levels of protein structure: primary, secondary, tertiary, and quaternary. Proteins can also be classified by their biological function, which includes enzymes, transport proteins, storage proteins, contractile/motile proteins, structural proteins, defense proteins, regulatory proteins, and other functional proteins. Classification by shape and solubility includes fibrous, globular, and membrane proteins. Classification by composition distinguishes between simple and conjugated proteins. Nutritionally, proteins are either complete or incomplete. The document concludes by discussing properties like denaturation and its causes like heat, alcohol, acids, bases, and heavy metal salts.
This document discusses amino acids, which are the building blocks of proteins. It defines amino acids as molecules containing both carboxyl and amine groups. There are over 300 amino acids found in nature, but only 22 are used as the standard building blocks in proteins. These standard amino acids differ in the side chain (R group) attached to their alpha carbon. Amino acids join together via peptide bonds to form protein chains. Proteins are essential to all living organisms and are formed through the process of translation.
Secondary Structure Of Protein (Repeating structure of protein)Amrutha Hari
This document discusses the structure of proteins at various levels. It describes the primary, secondary, tertiary, and quaternary structures. The secondary structures discussed in detail include the alpha helix, beta pleated sheet, random coil, collagen helix, and beta turn. The alpha helix and beta pleated sheet are stabilized by hydrogen bonding between amino acids. The collagen helix structure provides strength and is the main component of connective tissues. Genetic disorders like Ehlers-Danlos syndrome and osteogenesis imperfecta result from defects in collagen structures. Ramachandran plots are used to visualize allowed backbone dihedral angles in protein structures.
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.
Fatty acids are basic building blocks of lipids and are amphipathic molecules containing an even number of carbon atoms. They can be classified as saturated, monounsaturated, or polyunsaturated depending on whether they contain single or multiple carbon-carbon double bonds. Long-chain fatty acids are found in meats and fish while medium-chain fatty acids are found in coconut oil. Fatty acids play important roles in cell membranes and producing hormones and are obtained through the diet as essential fatty acids like omega-3 and omega-6 fatty acids. However, high intakes of trans fats and saturated fats can increase health risks such as cancer, heart disease, and diabetes.
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.
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.
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.
Metabolism of essential and non essential amino acids 20mariagul6
This document summarizes the metabolism of essential and non-essential amino acids in humans. It explains that non-essential amino acids can be synthesized in the body, while essential amino acids cannot and must come from diet. It describes the two main pathways of amino acid metabolism as transamination and deamination. Transamination transfers amino groups between amino acids, while deamination removes amino groups to form ammonia. The carbon skeletons of amino acids can be broken down into seven key intermediates, determining if the amino acid is glucogenic, ketogenic, or both. Genetic defects in amino acid metabolism pathways can cause serious disease.
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 complex biomolecules composed of amino acids. They 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 a single protein chain. Quaternary structure refers to the shape of proteins with multiple chains. Proteins are classified based on shape (globular or fibrous) and function (enzymes, hormones, etc.). They have various properties including solubility, hydrolysis, and denaturation.
Triacylglycerols are the main form in which animals store fat and are composed of glycerol bonded to three fatty acid chains. They are insoluble in water and primarily function as energy reserves, being stored in adipose tissue. Triacylglycerols can be either simple, containing the same fatty acid at each position, or mixed, containing different fatty acids. They undergo hydrolysis for digestion and energy release and can become rancid if exposed to air, moisture, or bacteria through oxidative or hydrolytic processes. Antioxidants help prevent rancidity.
This document discusses the chemistry of proteins and amino acids. It begins by explaining that proteins are abundant organic molecules that make up 50% of cellular mass and are essential for structure and function. The document then goes into detail about the classification, structure, properties and roles of the 20 standard amino acids that make up proteins. It describes how amino acids combine through peptide bonds to form polypeptide chains and proteins. The document provides a comprehensive overview of the biochemistry of proteins and amino acids.
Fatty acids play key roles in metabolism as fuels, for energy storage and transport, and as components of cell membranes. They are classified by their level of saturation. Saturated fatty acids have no double bonds while unsaturated fatty acids have one or more double bonds. The structure of fatty acids consists of a carboxyl end, alpha and beta carbons, and an omega methyl end. Fatty acids are broken down through beta-oxidation to produce acetyl-CoA for energy. They can also undergo lipid peroxidation or saponification.
This document defines and describes various types of lipids. It begins by explaining that lipids are a heterogeneous group of compounds related to fatty acids, fats, oils, waxes and other substances. It then discusses the basic components of lipids like fatty acids, glycerol and their esters known as triglycerides. The document further classifies lipids into simple lipids, compound lipids and derived lipids. Various types of phospholipids, glycolipids, sterols and terpenoids are also explained. Physical and chemical properties of lipids are outlined along with their important functions in living organisms.
The document provides information on amino acids including their history, classification, structure and properties. It discusses how amino acids were first discovered in 1806 and classified based on nutritional requirements, polarity, metabolic fate and structure. Key points include that amino acids have an amino group and carboxyl group, exist in ionized forms in biological systems, and 20 are used as building blocks of proteins. Their physical properties like solubility, isoelectric point and ability to act as ampholytes are also covered.
Amino acids are organic compounds that contain an amino group, a carboxyl group, a central carbon atom, and a side chain. There are 20 standard amino acids that are the building blocks of proteins. Amino acids can be classified based on their structure, polarity, nutritional requirements, and metabolic fate. They perform important functions including serving as monomers for protein synthesis, participating in cellular processes, and acting as precursors for other compounds.
This document discusses glycolipids, which are lipids that contain one or more sugar molecules. Glycolipids are classified as glycosphingolipids, globosides, gangliosides, and sulfatides. Glycosphingolipids contain ceramide and one or more sugars. Gangliosides contain sialic acid and contribute to cell membrane structure and function. Genetic defects that prevent the breakdown of glycolipids cause lipid storage diseases like Gaucher's disease and Tay-Sachs disease, leading to lipid accumulation in tissues and associated symptoms. Laboratory tests can diagnose these conditions by measuring enzyme levels or examining tissues. Some lipid storage diseases can be treated through enzyme replacement therapy.
Deamination and decarboxylation are processes that break down amino acids. Deamination removes an amine group from an amino acid, releasing ammonia. There are two types of deamination - oxidative deamination uses oxidation to remove the amine group, while non-oxidative uses other reactions. Decarboxylation removes a carboxyl group from an amino acid, releasing carbon dioxide. Both processes help convert excess amino acids into usable byproducts that can be removed from the body.
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.
This document provides information on beta-oxidation of fatty acids. It discusses the three stages of beta-oxidation: activation of fatty acids in the cytosol, transport into mitochondria via carnitine shuttle, and beta-oxidation in the mitochondrial matrix. The four reactions of each beta-oxidation cycle are also described: oxidation, hydration, oxidation, and cleavage. Deficiencies in beta-oxidation can cause conditions like sudden infant death syndrome.
Proteins are macromolecules made of amino acids linked by peptide bonds. They serve critical structural, functional, and regulatory roles in the body. Proteins have primary, secondary, tertiary and sometimes quarternary structures determined by their amino acid sequence. They perform diverse roles such as catalyzing biochemical reactions, transporting molecules, providing structure, and participating in immune defenses. Proteins are essential to the structure and function of all living organisms.
This document discusses proteins, including their structure, types, and functions. It notes that proteins are composed of amino acids, of which there are 20 common types. Proteins can have fibrous or globular structures depending on how the polypeptide chains are arranged. The structures of proteins include primary, secondary, tertiary, and sometimes quaternary structures. Examples of protein functions include digestion, transport, structure, signaling, defense, and storage. The document also discusses amino acid classification, protein denaturation, and the mechanism of enzyme catalysis.
This document discusses amino acids, which are the building blocks of proteins. It defines amino acids as molecules containing both carboxyl and amine groups. There are over 300 amino acids found in nature, but only 22 are used as the standard building blocks in proteins. These standard amino acids differ in the side chain (R group) attached to their alpha carbon. Amino acids join together via peptide bonds to form protein chains. Proteins are essential to all living organisms and are formed through the process of translation.
Secondary Structure Of Protein (Repeating structure of protein)Amrutha Hari
This document discusses the structure of proteins at various levels. It describes the primary, secondary, tertiary, and quaternary structures. The secondary structures discussed in detail include the alpha helix, beta pleated sheet, random coil, collagen helix, and beta turn. The alpha helix and beta pleated sheet are stabilized by hydrogen bonding between amino acids. The collagen helix structure provides strength and is the main component of connective tissues. Genetic disorders like Ehlers-Danlos syndrome and osteogenesis imperfecta result from defects in collagen structures. Ramachandran plots are used to visualize allowed backbone dihedral angles in protein structures.
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.
Fatty acids are basic building blocks of lipids and are amphipathic molecules containing an even number of carbon atoms. They can be classified as saturated, monounsaturated, or polyunsaturated depending on whether they contain single or multiple carbon-carbon double bonds. Long-chain fatty acids are found in meats and fish while medium-chain fatty acids are found in coconut oil. Fatty acids play important roles in cell membranes and producing hormones and are obtained through the diet as essential fatty acids like omega-3 and omega-6 fatty acids. However, high intakes of trans fats and saturated fats can increase health risks such as cancer, heart disease, and diabetes.
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.
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.
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.
Metabolism of essential and non essential amino acids 20mariagul6
This document summarizes the metabolism of essential and non-essential amino acids in humans. It explains that non-essential amino acids can be synthesized in the body, while essential amino acids cannot and must come from diet. It describes the two main pathways of amino acid metabolism as transamination and deamination. Transamination transfers amino groups between amino acids, while deamination removes amino groups to form ammonia. The carbon skeletons of amino acids can be broken down into seven key intermediates, determining if the amino acid is glucogenic, ketogenic, or both. Genetic defects in amino acid metabolism pathways can cause serious disease.
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 complex biomolecules composed of amino acids. They 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 a single protein chain. Quaternary structure refers to the shape of proteins with multiple chains. Proteins are classified based on shape (globular or fibrous) and function (enzymes, hormones, etc.). They have various properties including solubility, hydrolysis, and denaturation.
Triacylglycerols are the main form in which animals store fat and are composed of glycerol bonded to three fatty acid chains. They are insoluble in water and primarily function as energy reserves, being stored in adipose tissue. Triacylglycerols can be either simple, containing the same fatty acid at each position, or mixed, containing different fatty acids. They undergo hydrolysis for digestion and energy release and can become rancid if exposed to air, moisture, or bacteria through oxidative or hydrolytic processes. Antioxidants help prevent rancidity.
This document discusses the chemistry of proteins and amino acids. It begins by explaining that proteins are abundant organic molecules that make up 50% of cellular mass and are essential for structure and function. The document then goes into detail about the classification, structure, properties and roles of the 20 standard amino acids that make up proteins. It describes how amino acids combine through peptide bonds to form polypeptide chains and proteins. The document provides a comprehensive overview of the biochemistry of proteins and amino acids.
Fatty acids play key roles in metabolism as fuels, for energy storage and transport, and as components of cell membranes. They are classified by their level of saturation. Saturated fatty acids have no double bonds while unsaturated fatty acids have one or more double bonds. The structure of fatty acids consists of a carboxyl end, alpha and beta carbons, and an omega methyl end. Fatty acids are broken down through beta-oxidation to produce acetyl-CoA for energy. They can also undergo lipid peroxidation or saponification.
This document defines and describes various types of lipids. It begins by explaining that lipids are a heterogeneous group of compounds related to fatty acids, fats, oils, waxes and other substances. It then discusses the basic components of lipids like fatty acids, glycerol and their esters known as triglycerides. The document further classifies lipids into simple lipids, compound lipids and derived lipids. Various types of phospholipids, glycolipids, sterols and terpenoids are also explained. Physical and chemical properties of lipids are outlined along with their important functions in living organisms.
The document provides information on amino acids including their history, classification, structure and properties. It discusses how amino acids were first discovered in 1806 and classified based on nutritional requirements, polarity, metabolic fate and structure. Key points include that amino acids have an amino group and carboxyl group, exist in ionized forms in biological systems, and 20 are used as building blocks of proteins. Their physical properties like solubility, isoelectric point and ability to act as ampholytes are also covered.
Amino acids are organic compounds that contain an amino group, a carboxyl group, a central carbon atom, and a side chain. There are 20 standard amino acids that are the building blocks of proteins. Amino acids can be classified based on their structure, polarity, nutritional requirements, and metabolic fate. They perform important functions including serving as monomers for protein synthesis, participating in cellular processes, and acting as precursors for other compounds.
This document discusses glycolipids, which are lipids that contain one or more sugar molecules. Glycolipids are classified as glycosphingolipids, globosides, gangliosides, and sulfatides. Glycosphingolipids contain ceramide and one or more sugars. Gangliosides contain sialic acid and contribute to cell membrane structure and function. Genetic defects that prevent the breakdown of glycolipids cause lipid storage diseases like Gaucher's disease and Tay-Sachs disease, leading to lipid accumulation in tissues and associated symptoms. Laboratory tests can diagnose these conditions by measuring enzyme levels or examining tissues. Some lipid storage diseases can be treated through enzyme replacement therapy.
Deamination and decarboxylation are processes that break down amino acids. Deamination removes an amine group from an amino acid, releasing ammonia. There are two types of deamination - oxidative deamination uses oxidation to remove the amine group, while non-oxidative uses other reactions. Decarboxylation removes a carboxyl group from an amino acid, releasing carbon dioxide. Both processes help convert excess amino acids into usable byproducts that can be removed from the body.
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.
This document provides information on beta-oxidation of fatty acids. It discusses the three stages of beta-oxidation: activation of fatty acids in the cytosol, transport into mitochondria via carnitine shuttle, and beta-oxidation in the mitochondrial matrix. The four reactions of each beta-oxidation cycle are also described: oxidation, hydration, oxidation, and cleavage. Deficiencies in beta-oxidation can cause conditions like sudden infant death syndrome.
Proteins are macromolecules made of amino acids linked by peptide bonds. They serve critical structural, functional, and regulatory roles in the body. Proteins have primary, secondary, tertiary and sometimes quarternary structures determined by their amino acid sequence. They perform diverse roles such as catalyzing biochemical reactions, transporting molecules, providing structure, and participating in immune defenses. Proteins are essential to the structure and function of all living organisms.
This document discusses proteins, including their structure, types, and functions. It notes that proteins are composed of amino acids, of which there are 20 common types. Proteins can have fibrous or globular structures depending on how the polypeptide chains are arranged. The structures of proteins include primary, secondary, tertiary, and sometimes quaternary structures. Examples of protein functions include digestion, transport, structure, signaling, defense, and storage. The document also discusses amino acid classification, protein denaturation, and the mechanism of enzyme catalysis.
Protein is a macronutrient that is essential to building muscle mass. It is commonly found in animal products, though is also present in other sources, such as nuts and legumes. There are three macronutrients: protein, fats and carbohydrates. Macronutrients provide calories, or energy.
Proteins are organic macromolecules made of amino acids linked by peptide bonds. They range widely in size and function. The fundamental units are 20 different amino acids that make up the primary structure in different sequences. Secondary structures like alpha helices and beta sheets form due to hydrogen bonding of amino acid R groups. Tertiary and quaternary structures arise from further folding and interactions between polypeptide subunits. Proteins have important roles like enzymatic catalysis, transport, structure, regulation and defense. They are classified based on solubility and presence of non-protein groups.
The document discusses proteins and polypeptides. It defines proteins as polymers of amino acids that perform important structural and functional roles in the body. Proteins are classified based on shape, constitution and nature. Polypeptides are continuous chains of amino acids joined by peptide bonds. They are precursors to proteins and are synthesized through a process involving transcription and translation. Common methods for synthesizing polypeptides include Fischer's method which uses protecting groups to join amino acids, and modifications of this method.
Proteins are made up of chains of amino acids that fold into complex 3D shapes defined by their sequence. There are 20 types of amino acids that can be combined to form the primary structure of a protein. The sequence determines the unique secondary, tertiary, and sometimes quaternary structures which define a protein's specific function. Proteins perform most of the work in cells and have roles in structure, function, regulation and catalysis. The seven main types of proteins include enzymes, structural proteins, transport proteins and more, each with distinct functions in the body.
Proteins play many important biochemical roles in the body. They act as enzymes, hormones, antibodies, and structural components. Proteins can be classified based on their shape (fibrous or globular) or chemical composition (simple or conjugated). Simple proteins only contain amino acids, while conjugated proteins also contain non-amino acid groups like nucleic acids, lipids, carbohydrates, or metals. Proteins are further classified as complete or incomplete based on whether they contain all essential amino acids.
This document discusses the structural hierarchy of proteins from primary to quaternary structure. It explains that proteins are made up of amino acids linked together in polypeptide chains. The primary structure is the sequence of amino acids in the chain. Secondary structures like alpha helices and beta sheets form due to hydrogen bonding. Tertiary structure is the 3D folding of secondary structures into the lowest energy state. Quaternary structure involves multiple polypeptide chains combining to form oligomeric proteins. The document also classifies proteins based on shape and constitution and discusses the functions of different types of proteins like enzymes, hormones, and structural proteins.
This document provides information about proteins presented in a biochemistry lecture. It defines proteins as macromolecules made of amino acid polymers. 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. Tertiary structure involves protein folding into three-dimensional shapes. Quaternary structure involves interactions between protein subunits. Examples discussed are hemoglobin, which carries oxygen in red blood cells, and myoglobin, which stores oxygen in muscle cells. Both contain heme but hemoglobin transports oxygen while myoglobin stores it.
The document provides information about proteins including their introduction, chemical nature, physical properties, structure, classification, and functions. Some key points:
- Proteins are macromolecules composed of amino acid chains that serve important structural and functional roles in the body.
- They have complex hierarchical structures ranging from primary sequences to quaternary arrangements and take on globular or fibrous shapes.
- Proteins can be classified based on their shape, composition, solubility, and biological function. This includes categories like enzymes, structural proteins, and transport proteins.
- In addition to providing structure, proteins regulate body chemistry through roles as hormones, antibodies, and contractile proteins involved in muscle movement.
Proteins are made up of amino acid monomers linked together by peptide bonds. They are synthesized through transcription and translation processes involving DNA, RNA and ribosomes. Proteins have four levels of structure - primary, secondary, tertiary and quaternary - which determine their shape and function. Proteins perform many essential roles in cells and organisms such as catalysis, structure, defense and transport.
Proteins are composed of chains of amino acids linked together by peptide bonds. There are 20 common amino acids that make up proteins. The sequence of amino acids is determined by the DNA sequence. Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. Proteins serve many important functions in the body such as catalysis, muscle contraction, cytoskeleton structure, transport, cell signaling, and immunity.
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A presentation slide on Peptides and Proteins. Presented in the Course CHE-109 in East West University.
This document provides information about proteins in 3 paragraphs:
1) It defines proteins as organic compounds made of amino acid chains that form complex 3D shapes and serve essential functions in living organisms. They are the most abundant organic compounds in cells.
2) It describes the 4 levels of protein structure from primary to quaternary, where the amino acid sequence determines the overall 3D shape through coiling and folding.
3) It briefly mentions the 20 common amino acids that make up proteins and the formation of peptide bonds between amino acid units.
1) The document discusses food proteins and enzymes, their importance in biological systems, and their various functions and sources.
2) Proteins are made up of amino acids and play many critical roles including as enzymes, hormones, antibodies, and structural components.
3) The document covers the classification of amino acids, sources of food proteins like meat and dairy, and the roles of enzymes in catalyzing biochemical reactions.
The document discusses several key biological molecules including amino acids, proteins, DNA and RNA. It provides information on their structures and functions. Specifically, it explains that amino acids combine to form proteins, and that DNA and RNA are made up of nucleotides that contain nitrogenous bases and form structures through hydrogen bonding. The roles of these molecules in processes like protein synthesis and gene expression are also summarized.
Quaternary structure refers to the arrangement of multiple protein subunits into a single protein complex. Hemoglobin is a common example that is made of two alpha and two beta subunits. The subunits interact through hydrophobic interactions, hydrogen bonding, and other bonds. Globular proteins tend to have quaternary structure that clusters the subunits into a spherical shape, while fibrous proteins form long coils or sheets through interactions between subunits. Quaternary structure allows proteins to take on specialized functions beyond what individual subunits could achieve alone.
Similar to Protein Classification & Features By Syekat (20)
An oil spill is a release of crude oil or refined petroleum products into the environment, such as oceans, rivers, lakes, or land. Oil spills can be caused by a variety of factors, including accidents during transportation, storage, or drilling operations, natural disasters such as hurricanes or earthquakes.
The primary productivity of phytoplankton, macroalgae, and seagrasses forms the base of marine ecosystem structuring in aquatic environments. Primary productivity is affected by various environmental factors and ecological processes that usually interact in a complex manner. The rate of primary production usually governs the overall ecosystem health and ecological productivity of a water body, and any observed trends may reveal the occurrence of potential stresses on existing ecosystems. Along the Saudi Gulf coast, primary productivity monitoring may help provide the basis for identifying the potential stressors to the coastal marine environments. Foremost among the considerations is the potential adverse effect of excessive anthropogenic nutrient loadings, which may lead to eutrophication events that can adversely impact on ecosystem health. In addition, high nutrient loads from man-made activities may trigger the excessive growth of some toxic phytoplankton species, potentially resulting in harmful algal blooms (HABs) with serious human health risks and negative economic impacts.
This study is geared towards monitoring the primary productivity levels in selected areas of the Saudi Gulf waters to identify areas of concern as regards hyper-nutrification, ecological disturbance, and potential hot spots for HAB events. Nutrient loadings and the identification of potential HAB organisms will form a special focus of the investigations.
Carbon is an essential element for all life forms on Earth. Whether these life forms
take in carbon to help manufacture food or release carbon as part of respiration, the
intake and output of carbon is a component of all plant and animal life.
The carbon cycle is vital to life on Earth. Nature tends to keep carbon levels balanced,
meaning that the amount of carbon naturally released from reservoirs is equal to the
amount that is naturally absorbed by reservoirs. Maintaining this carbon balance
allows the planet to remain hospitable for life. Scientists believe that humans have
upset this balance by burning fossil fuels, which has added more carbon to
the atmosphere than usual and led to climate change and global warming.
This document provides information about aerators and their design in aquaculture farms and hatcheries. It discusses why aeration is needed, the benefits of aerators, the basic principles of aeration, and different types of aerators and their designs. The main types of aerators described are vertical pumps aerators, surface aerators, pump sprayers, propeller-aspirator pumps, paddlewheel aerators, and diffused-air systems. Each type is explained in terms of its design, construction, advantages, and disadvantages. The overall purpose is to outline various aerator options and considerations for aquaculture operations.
Global production from aquaculture is growing substantially and provides increasingly significant volumes of fish and other aquatic food for human consumption, a trend that is projected to continue. Although aquaculture growth has potential to meet the growing need for aquatic foods and to contribute to food security, poverty reduction and, more broadly, to achieving sustainable development and the Millennium Development Goals, it is increasingly recognized that improved management of the sector is necessary to achieve this potential. The application of certification in aquaculture is now viewed as a potential market-based tool for minimizing potential negative impacts and increasing societal and consumer benefits and confidence in the process of aquaculture production and marketing
Reproduction is a fundamental biological process which enables continuation of species. In fisheries biology, reproduction assumes greater significance to understand sexual
dimorphism, process of maturation, size or age of maturity, breeding season, spawning area, sexual segregation, migration, fecundity, embryonic and larval development and
recruitment. Most of the management strategies in capture fisheries are based on reference points that are the manifestations of reproductive biology. In aquaculture,
knowledge of reproductive biology of a fish is essential for hatchery production of fish feeds.
,
Nazmul Haque Syekat
Whiteleg shrimp (Litopenaeus vannamei, formerly Penaeus vannamei), also known as Pacific white shrimp or King prawn, is a variety of prawn of the eastern Pacific Ocean commonly caught or farmed for food.L. vannamei is a decapod crustacean which is native to the Eastern Pacific Coast of Central and
South America from Tumbes, Peru in the south to Mexico in the north. It has been introduced widely around the world since the 1970s, but especially since 2000, as it has become the principle
cultured shrimp species in Asia. The species itself is not considered a major threat to biodiversity, does not appear to have formed breeding populations, and has generally resulted in positive economic impacts in non-indigenous areas. An examination of current lists of invasive species
published by the International Union for Conservation of Nature’s Invasive Species Specialist Group (IUCN, 2004) revealed no listings for L. vannamei. As mentioned, L. vannamei has been anthropogenically introduced as an aquaculture species to several areas of the world to which it is
not native.
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Nazmul Haque Syekat
Haploids are individuals that have only a single set of chromosomes. Because they have only a single set of chromosomes, every detrimental allele will be expressed, since none will be hidden by a dominant allele in the heterozygous condition. As such, it is doubtful that many haploids will survive very long. Haploid medaka , common carp , masu salmon , rainbow trout , Atlantic salmon , chum salmon and plaice have been produced for experimental purposes, but none lived long.
The government of Bangladesh has formulated the Government Water Resources Management Policy, 2009 in the public interest with a view to giving priority to the provision of settlements in favor of real fishermen and conservation of biodiversity including conservation of fishery resources and increase in production.
Blue Economy means sustainable use of ocean resources for economic growth, improved livelihoods and jobs, and ocean environment health. More specifically, it basically refers to any economic activity in the marine sector, whether sustainable or not”.In Bangladesh , Coastal and Marine based aquaculture has been developed day by day .There are many prawn and shrimp farm in Bangladesh among the different districts.These farm play a dominant role for rising blue economic development of Bangladesh .Besides sea weed is also a prominent aquaculture in Bangladesh .There are about 133 species of sea weeds that commercially produce in different kinds of farm in Bangladesh .Although there has so many bar to management theses types of farm ,but day by day the efficiency of producing these product are increasing very rapidly. A very great role has kept by the marine and coastal aquaculture for developing blue economy of Bangladesh
Inbreeding is the production of offspring from the mating or breeding of individuals or
organisms that are closely related genetically.By analogy, the term is used in human
reproduction, but more commonly refers to the genetic disorders and other consequences that
may arise from expression of deleterious or recessive traits resulting from incestuous sexual
relationships and consanguinity. Inbreeding results in homozygosity, which can increase the
chances of offspring being affected by deleterious or recessive traits.This usually leads to at least
temporarily decreased biological fitness of a population(called inbreeding Common fruit fly
females prefer to mate with their own brothers over unrelated males. depression), which is its
ability to survive and reproduce. An individual who inherits such deleterious traits is colloquially
referred to as inbred. The avoidance of expression of such deleterious recessive alleles caused by
inbreeding, via inbreeding avoidance mechanisms, is the main selective reason for outcrossing.
Crossbreeding between populations also often has positive effects on fitnessrelated traits, but
also sometimes leads to negative effects known as outbreeding depression. However increased
homozygosity increases probability of fixing beneficial alleles and also slightly decreases
probability of fixing deleterious alleles in population. Inbreeding can result in purging of
deleterious alleles from a population through purifying selection.
Bangladesh , the largest delta on earth, is situated
in South Asia. It is located between 20°
34′ and
26°
38′ north latitude and 88°
01′ and 92°
41′ east
longitude. It is bordered by India on the west,
north, and east, by Myanmar on the southeast, and
by the Bay of Bengal on the south. The area of the
country is 147,570 km2
. Most of the country is
low-lying comprising mainly the delta of the
Ganges and Brahmaputra rivers. A total of 80% of
the country is floodplain . The environment of the
country is under severe pressure due to changing
climate and destructive anthropogenic activities.
Environmental degradation is directly and
indirectly affecting human health, ecosystems
, and economic growth of the country. Demographic pressure, poverty,lack of proper
awareness on environmental issues, and lack of implementation and monitoring of
environmental rules are the main causes for existing environmental condition of
Bangladesh. The climatic condition of Bangladesh is tropical monsoon. The country
currently faces several environmental issues which threaten these resources, including
groundwater metal contamination, increased groundwater salinity, cyclones and flooding, and
sedimentation and changing patterns of stream flow due to watershed mismanagement. Some
of these, such as the changing patterns of stream flow and presence of lead in groundwater,
can be directly correlated with human activity and industrial processes, while others, such as
cyclones and flooding are naturally occurring issues.
Geographic environment is that part of the terrestrial natural environment
that has been to some extent altered by human beings and which at the
present moment is directly connected with the life and production activity
of society. The natural objects and the phenomena related to them which
surround men constitute the geographical environment. (eg. surface of the
earth, minerals, water, animals, mountains, plants, sun, moon, plains.) The
geographic environment is one of the permanent and necessary conditions
for the development of society. It can accelerate or retard this development,
but it is not the main moving force of society’s development, since the
specific laws of the movement of nature and society, as well as the rates of
movement (changes), are essentially different.
This document provides information on different types of parasites that infect fish, including protozoa, monogenean trematodes, digenean trematodes, nematodes, cestodes, and parasitic crustacea. It describes the key characteristics and impacts of common parasites within each group, such as ichthyobodo flagellates, trichodina ciliates, gyrodactylus and dactylogyrus monogeneans, and ergasilus crustaceans. The document emphasizes that while some parasites may cause little issue, heavy infestations can damage tissues, remove fluids, weaken the fish's health, and allow secondary infections.
Social impact assessment (SIA) includes the processes of analyzing, monitoring and managing
the intended and unintended social consequences, both positive and negative, of planned
interventions (policies, programs, plans, projects) and any social change processes involved by
those interventions ( According to the International Association for Impact Assessment).In case
of fisheries science Social Impact Assessment is a method of gauging the social and cultural
consequences of alternative fishery management actions or policies. The purpose and logic of the
SIA are the same as those for the economic and ecological elements of environmental impact
analysis and assessment. An impact assessment determines (social/cultural) conditions in areas
or populations likely to be affected by the regulatory action or policy; projects future effects of
continuing the status quo; and then estimates effects, relative to the status quo, that will result on
local, regional, and national scales if reasonable fishery management alternatives are
implemented.
Fish diseases affect the survival and growth rates of fìsh under culture. Given that drug
treatments are expensive, fìsh diseases invariably lead to lower harvest and higher cost.
Fish farmers often suffer hefty economic losses due to fìsh diseases.To alleviate such losses,
it is crucial to take precautions to prevent fìsh diseases and reduce pathogen levels in water
bodies. It is also important to prevent water quality from deteriorating and to strengthen
the natural resistance of the fìsh stock. Regular monitoring of fìsh health is an effective way
to identify disease causes and appropriate treatments. One major cause of serious fìsh kill
is overlooking the contagiousness of fìsh diseases and thus delaying treatment. As such,
adequate care and treatment should be given to infected fish promptly.
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Nazmul Haque Syekat
Syekat
Four fishing grounds have been identified so far. They are south patches, south of south patches, middle ground and Swatch of no Ground.This slide will show you about the different fishing site in bay of bengal where the abundance of fish is higher than other areas.
This document provides details from a field work trip to Saint Martin Island in Bangladesh. It includes acknowledgements, a table of contents, an introduction to the island, and descriptions of experiments conducted to measure water quality parameters, collect benthos, and identify seaweed samples. 9 species of seaweed were identified from samples collected on the trip. The conclusion discusses the biodiversity and ecosystems of the island and threats they face from pollution and lack of proper management.
This document provides an overview of biosensors. It defines a biosensor as an analytical device that combines a biological component with a physicochemical detector to detect a chemical substance. The biological component is typically an enzyme, antibody, or nucleic acid. Biosensors have three main components: a bioreceptor that recognizes the target analyte, a transducer that converts the biorecognition event into a measurable signal, and electronics that process and display the signal. The document discusses the characteristics, types, applications, and advantages of biosensors, noting their use in healthcare, environmental monitoring, food analysis, and other areas due to their rapid detection, high specificity, and minimal reagent requirements.
The document discusses the characteristics, types, habitats, behaviors, threats and other aspects of manatees. It describes how there are three main types of manatees found in warm tropical waters around the world. The document provides details on manatee anatomy, feeding habits, reproduction, communication, and threats they face such as habitat loss, hunting, and collisions with boats.
More from Nazmul Haque Syekat, Noakhai Science & Technology University. (20)
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Disclaimer: No one is perfect, so please mind that there might be mistakes and typos.
dtubbenhauer@gmail.com
Corrected slides: dtubbenhauer.com/talks.html
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Protein Classification & Features By Syekat
1. Noakhali Science And Technology University
NAZMUL HAQYE SYEKAT
FISHERIES AND MARINE SCIENCE
NOAKHALI SCIENCE AND
TECHNOLOGY UNIVERSITY.
PHONE NO:01728113120
2. Introduction to Protein.
Definition of Protein.
Feature of Protein.
Properties of protein.
Classification of Protein .
Structure of Protein .
Function of Protein.
Conclusion
3. Proteins are important molecules of
cells.Protein are the major component of
the dry weight of cells.
The name was first sugggested in 1838 by
a swedish chemist Berzelous.
Protein are known as the building blocks
of life .Protein are consist on one or more
chains of amino acid.
4. Protein is a complex organic nitrogenous
compound composed of amino acid
linked together by peptide bonds.
Protein is a high molecular-weight
polypeptide made up of amino acid linked
together by polypeptide bonds.
5. Most important biomolecules. they are the
fundamental constituent of the cytoplasm of the
cell.
Structural elements of body tissues.
Proteins are considered as the bricks, they make
up bones, muscles, hair and other parts of the body.
Proteins like enzymes are functional elements that
take part in metabolic reactions.
Antibodies, blood haemoglobin are also made of
proteins.
6. Physical Properties…
Proteins are colorless and tasteless.
They are homogeneous and crystalline.
Proteins vary in shape, they may be simple
crystalloid structure to long fibrilar structures.
The diffusion rates of proteins is extremely
slow.
Proteins exhibit Tyndall effect.
7. Hydrolyzed by acidic agents.
Reaction with alcohols & gives esters.
This process is known as esterification.
Amino acids reacts with amines to form
amides.
Protein gives Sanger reaction.
Protein gives Xanthoproteic Test.
Protein gives Folin’s test.
8. Three types of Protein
Simple Protein
Protein
Conjugated
Protein
Derived
Protein
9. These proteins are made of only one type of amino
acid, as structural component, on decomposition
with acids, they liberate constituent amino
acids.Simple proteins are further classified based
on their solubility.
Name Example
Albumins Leucosine, legumeline, serum albumin
Globulins Pseudoglobulin, serum globulin, glycinine
Protamines salmine, clupine, cyprinine
Histones nucleoshistones, globin.
Scleroproteins Animal skeleton proteins.
10. These are proteins that are made of amino acids
and other organic compounds. The non-amino acid
group is termed as prosthetic group. Complex
proteins are further classified based on the type of
prosthetic group present.
Name Example
Metalloproteins casein, collagen, ceruloplasmin
Chromoproteins Myoglubin, hemocyanin, cytochromes
Glycoproteins egg albumin, serum globulins, Mucoproteins
Phosphoproteins casein
Lipoproteins lipovitellin, lipoproteins of blood
Nucleoproteins Nucleoproteins, nucleohistones, nuclein.
11. These are proteins that are derived from the action
of heat, enzyme or chemical reagents.Derived
proteins are of two types, primarily derived proteins
and secondary derived proteins.
Primary derived proteins are classified into three
types: - Proteans, Infraproteins and Coagulated
proteins. Example: edestan, coagulated eggwhite.
Secondary derived proteins are further classified
into 3 types: - Proteoses, Peptones and
Polypeptides.
13. Primary Structure of Protein:
Primary structure of protein is the linear
sequence of amino acids that make up the
polypeptide chain.
His sequence is given by the sequence of
nucleotide bases of the DNA in the genetic
code.
Secondary Structure of Protein:
The folding of the polepeptide chain into a
specific coiled structure held together by
disulfide bonds and hydrogen bonds is
knows as the secondary structure of
protein.
14. Tertiary Structure of Protein:
Tertiary structure of proteins is the three
dimensional structure formed by the bending and
twisting of the polypeptide chain.The overall
arrangement and interrelationship of the various
regions, or domain and individual amino acid
residues of a single polypeptide chain is known as
the tertiary structure of protein.
Quaternary Structure of Protein:
Some proteins contain more than one polypeptide
chains, this association of polypeptide chains refers
to the quaternary structure.Each polypeptide chain
is called a subunit.
15. Found in muscles, hair, skin and
other tissues, E.g: keratin, is
present in nails and hair.
Some protein act as hormones
Example: Insulin hormone.
Act as enzymes. E.g: Pepsin and
Tripsin.
Act as antibodies.
16. Transport substances in blood of
different tissues. E.g: Haemoglobin
is a oxygen transport protein.
Contraction of muscle and cells .E.g:
Myosin.
Prevents blood loss.E.g:Fibrinogen.
17. At last now we are clearly informed about
the Protien,what's it and what it's
Features and properties,what it's
important along to our body.Protein are
the most essential element for our body.It
can be uses For developing our body in
various purpose.
18.
19. This is my first powerpoint presentation of my university life.