Biochemistry-PROTEINS
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The document discusses proteins, which are made up of amino acids linked together by peptide bonds. Proteins fold into complex three-dimensional shapes determined by interactions between amino acid side chains. This folding allows proteins to carry out specific biological functions. The folding process and levels of protein structure, from primary to quaternary, are described. Two main types of proteins, globular and fibrous, are also mentioned.
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Chemistry of amino acids
Amino acids are the building blocks of proteins. There are 20 standard amino acids that make up proteins. Amino acids have a general structure that includes an amino group, a carboxyl group, and a side chain. They can be classified based on their structure, side chain properties, nutritional requirements, and metabolic fate. Common properties of amino acids include being crystalline solids, existing as zwitterions with an isoelectric point, and having chirality with L and D isomers. Amino acids undergo various reactions due to their amino, carboxyl, and side chain groups.
Proteins-Classification ,Structure of protein, properties and biological impo...
This document provides an overview of proteins, including their definition, classification, structure, and properties. It discusses how proteins are composed of amino acids and classified based on their chemical nature, structure, shape and solubility. The four levels of protein structure - primary, secondary, tertiary, and quaternary structure - are also summarized. Key properties of proteins like solubility, denaturation and functions in the body are highlighted. The document serves as an introduction to proteins and provides a high-level classification and structural overview.
Biological roles of proteins
Proteins play very significant role in cell functioning. they are known as workhorse of cell. they are made up of amino acids.
Classification of protein
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.
Structure of protein
This document summarizes the four levels of protein structure: primary, secondary, tertiary, and quaternary. It provides details on each level: primary structure refers to the linear sequence of amino acids in the polypeptide chain. Secondary structure involves hydrogen bonding between amino acids to form regular structures like alpha helices and beta pleated sheets. Tertiary structure describes the overall 3D shape of the protein arising from secondary structures. Quaternary structure involves interactions between two or more polypeptide chains, as seen in hemoglobin which is made of four polypeptide subunits.
Classification of Protein by different mode.
• 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
Classification and properties of protein
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.
Types of RNA
RNA comes in several types that serve different functions. Messenger RNA (mRNA) acts as a template for protein synthesis by carrying genetic code from DNA to the ribosomes. Transfer RNA (tRNA) transfers amino acids to the ribosome during protein synthesis. Ribosomal RNA (rRNA) is a core component of ribosomes and catalyzes peptide bond formation. Other non-coding RNAs include microRNAs (miRNAs) that regulate gene expression at the post-transcriptional level, and small nuclear RNAs (snRNAs) that are involved in splicing mRNA transcripts. RNAs play essential roles in coding, decoding, regulating, and expressing genes.
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Chemistry of amino acids
Amino acids are the building blocks of proteins. There are 20 standard amino acids that make up proteins. Amino acids have a general structure that includes an amino group, a carboxyl group, and a side chain. They can be classified based on their structure, side chain properties, nutritional requirements, and metabolic fate. Common properties of amino acids include being crystalline solids, existing as zwitterions with an isoelectric point, and having chirality with L and D isomers. Amino acids undergo various reactions due to their amino, carboxyl, and side chain groups.
Proteins-Classification ,Structure of protein, properties and biological impo...
This document provides an overview of proteins, including their definition, classification, structure, and properties. It discusses how proteins are composed of amino acids and classified based on their chemical nature, structure, shape and solubility. The four levels of protein structure - primary, secondary, tertiary, and quaternary structure - are also summarized. Key properties of proteins like solubility, denaturation and functions in the body are highlighted. The document serves as an introduction to proteins and provides a high-level classification and structural overview.
Biological roles of proteins
Proteins play very significant role in cell functioning. they are known as workhorse of cell. they are made up of amino acids.
Classification of protein
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.
Structure of protein
This document summarizes the four levels of protein structure: primary, secondary, tertiary, and quaternary. It provides details on each level: primary structure refers to the linear sequence of amino acids in the polypeptide chain. Secondary structure involves hydrogen bonding between amino acids to form regular structures like alpha helices and beta pleated sheets. Tertiary structure describes the overall 3D shape of the protein arising from secondary structures. Quaternary structure involves interactions between two or more polypeptide chains, as seen in hemoglobin which is made of four polypeptide subunits.
Classification of Protein by different mode.
• 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
Classification and properties of protein
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.
Types of RNA
RNA comes in several types that serve different functions. Messenger RNA (mRNA) acts as a template for protein synthesis by carrying genetic code from DNA to the ribosomes. Transfer RNA (tRNA) transfers amino acids to the ribosome during protein synthesis. Ribosomal RNA (rRNA) is a core component of ribosomes and catalyzes peptide bond formation. Other non-coding RNAs include microRNAs (miRNAs) that regulate gene expression at the post-transcriptional level, and small nuclear RNAs (snRNAs) that are involved in splicing mRNA transcripts. RNAs play essential roles in coding, decoding, regulating, and expressing genes.
Protein structure, Protein unfolding and misfolding
Protein structure- Four levels of the organization of protein structure; Primary, secondary, tertiary and quaternary protein structure.
Biochemistry lecture notes proteins
Proteins have four levels of structure - primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structures include alpha helices and beta pleated sheets formed by hydrogen bonding between amino acid residues. Tertiary structure involves folding of the chain into a three-dimensional shape determined by interactions between R groups. Quaternary structure refers to complexes of multiple polypeptide subunits held together by various bonds and interactions. Hemoglobin is an example of a protein with quaternary structure, consisting of four subunits - two alpha chains and two beta chains.
Protein sturucture
This document discusses protein structure and function. It begins by defining proteins and their essential roles in the human body. It then describes the general characteristics of proteins, such as their chemical composition and functions. The document classifies proteins based on their composition, axial ratio, and biological functions. It explains the different levels of protein structure from primary to quaternary, focusing on secondary structure elements like alpha helices and beta sheets. The roles of hydrogen bonding, disulfide bridges, and ionic bonds in tertiary and quaternary structure are also described.
Proteins
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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.
Amino acid
Amino acids are organic compounds that contain an amino group, a carboxyl group, a central carbon atom, and a specific side chain. They are classified as essential, non-essential, or conditional depending on whether the human body can synthesize them. Amino acids are the building blocks of proteins and participate in many important biological functions and cellular processes. They have various physical and chemical properties depending on their specific structure and side chain, and many amino acids have medicinal properties and play roles in treating diseases.
Tertiary structure of proteins
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.
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Peptides
Peptides are short chains of amino acids linked by peptide bonds. They are distinguished from proteins by typically containing fewer than 50 amino acid units. Peptides are formed through condensation reactions between carboxyl and amino groups of separate amino acids, releasing a water molecule. Peptide bonds are rigid and planar, contributing to protein structure stability. Peptides serve many important biological functions and can be classified based on their production method, including through ribosomal translation, nonribosomal synthesis, and enzymatic digestion of proteins in foods. Bioactive peptides derived from food proteins can have beneficial effects like lowering blood pressure, cholesterol, and antimicrobial properties.
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The document provides information about amino acids and their classification. It discusses that amino acids are the monomer units that make up protein polymers. They can be classified based on their structure, side chains, nutritional requirements, and metabolic fate. The 20 standard amino acids are discussed in detail, including their physical and chemical properties. Key reactions of amino acids involving their amino, carboxyl, and side chain groups are also summarized.
Proteins ppt
Protein is an important component of every cell in the body. Hair and nails are mostly made of protein. Your body uses protein to build and repair tissues. You also use protein to make enzymes, hormones, and other body chemicals. Protein is an important building block of bones, muscles, cartilage, skin, and blood.
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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.
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Amino acids
This document discusses amino acids and their properties. It begins by explaining that amino acids are organic compounds that contain amine and carboxyl groups and have different R groups. Proteins are composed of chains of amino acids linked by peptide bonds. There are 20 standard amino acids that are the building blocks of proteins. The document then classifies amino acids based on their R groups and discusses their structures, chemical properties, and roles in the body.
Proteins.pptx
This document discusses proteins and was written by Dr. Kayeen Vadakkan, an assistant professor from St. Mary's College Thrissur, Kerala, India. It covers the classification, structure, and functions of proteins. Proteins can be classified based on their function, chemical nature and solubility, and nutritional properties. The structure of proteins includes primary, secondary, tertiary, and quaternary levels. Primary structure is the amino acid sequence, secondary involves folding patterns like alpha helices and beta sheets, tertiary is the three-dimensional structure, and quaternary involves interactions of subunits.
digestion and absorption of proteins.pptx
digestion and absorption of proteins
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This document discusses protein structure and function. It begins by defining proteins and their essential roles in the human body. It then describes the general characteristics of proteins, such as their chemical composition and functions. The document classifies proteins based on their composition, axial ratio, and biological functions. It explains the different levels of protein structure from primary to quaternary, focusing on secondary structure elements like alpha helices and beta sheets. The roles of hydrogen bonding, disulfide bridges, and ionic bonds in tertiary and quaternary structure are also described.
Proteins
Proteins are essential macromolecules that make up 20% of the human body. They are composed of amino acids and perform many critical functions including structure, regulation, catalysis, movement and more. Protein synthesis occurs in ribosomes within cells. Proteins are not stored but are broken down if excess amino acids are consumed. They have primary, secondary, tertiary and quaternary levels of structure determined by amino acid sequence and interactions. There are 20 standard amino acids that are linked by peptide bonds to form proteins.
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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.
Amino acid
Amino acids are organic compounds that contain an amino group, a carboxyl group, a central carbon atom, and a specific side chain. They are classified as essential, non-essential, or conditional depending on whether the human body can synthesize them. Amino acids are the building blocks of proteins and participate in many important biological functions and cellular processes. They have various physical and chemical properties depending on their specific structure and side chain, and many amino acids have medicinal properties and play roles in treating diseases.
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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.
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This document provides an overview of nucleotide biosynthesis. It discusses that nucleotides are composed of nitrogenous bases, pentose sugars, and phosphate groups, and are the building blocks of nucleic acids. There are two pathways for nucleotide biosynthesis - de novo synthesis which uses metabolic precursors to build nucleotides from scratch, and salvage pathways which recycle bases and nucleosides from nucleic acid breakdown. Key steps in purine and pyrimidine synthesis are described. Nucleotides have important biological functions as components of nucleic acids, energy carriers, and signaling molecules.
Peptides
Peptides are short chains of amino acids linked by peptide bonds. They are distinguished from proteins by typically containing fewer than 50 amino acid units. Peptides are formed through condensation reactions between carboxyl and amino groups of separate amino acids, releasing a water molecule. Peptide bonds are rigid and planar, contributing to protein structure stability. Peptides serve many important biological functions and can be classified based on their production method, including through ribosomal translation, nonribosomal synthesis, and enzymatic digestion of proteins in foods. Bioactive peptides derived from food proteins can have beneficial effects like lowering blood pressure, cholesterol, and antimicrobial properties.
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The document provides information about amino acids and their classification. It discusses that amino acids are the monomer units that make up protein polymers. They can be classified based on their structure, side chains, nutritional requirements, and metabolic fate. The 20 standard amino acids are discussed in detail, including their physical and chemical properties. Key reactions of amino acids involving their amino, carboxyl, and side chain groups are also summarized.
Proteins ppt
Protein is an important component of every cell in the body. Hair and nails are mostly made of protein. Your body uses protein to build and repair tissues. You also use protein to make enzymes, hormones, and other body chemicals. Protein is an important building block of bones, muscles, cartilage, skin, and blood.
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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.
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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.
Enzyme inhibition AND ITS TYPES
This document discusses enzyme inhibition. It defines inhibitors as substances that bind to enzymes and interfere with their activity, preventing the formation of enzyme-substrate complexes or their breakdown into products. There are two main types of inhibitors - reversible inhibitors, which bind non-covalently and can dissociate, and irreversible inhibitors, which bind covalently and permanently inactivate the enzyme. Reversible inhibition is further divided into competitive, uncompetitive and non-competitive inhibition based on whether the inhibitor binds the enzyme, enzyme-substrate complex, or both. Irreversible inhibitors permanently alter the enzyme's active site groups essential for activity. Examples of different types of inhibitors are provided.
Amino acids
This document discusses amino acids and their properties. It begins by explaining that amino acids are organic compounds that contain amine and carboxyl groups and have different R groups. Proteins are composed of chains of amino acids linked by peptide bonds. There are 20 standard amino acids that are the building blocks of proteins. The document then classifies amino acids based on their R groups and discusses their structures, chemical properties, and roles in the body.
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Proteins.pptx
This document discusses proteins and was written by Dr. Kayeen Vadakkan, an assistant professor from St. Mary's College Thrissur, Kerala, India. It covers the classification, structure, and functions of proteins. Proteins can be classified based on their function, chemical nature and solubility, and nutritional properties. The structure of proteins includes primary, secondary, tertiary, and quaternary levels. Primary structure is the amino acid sequence, secondary involves folding patterns like alpha helices and beta sheets, tertiary is the three-dimensional structure, and quaternary involves interactions of subunits.
digestion and absorption of proteins.pptx
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Protein motif. by KK Sahu sir
Introduction:
Protein
Protein motif.
2. History:
3. A brief overview of protein structure.
4. The Structural Classification of Protein(SCOP):
All α.
All β
α/β
α+β
5.The super secondary structure.
6. Rules for formation of Protein Motifs.
7. Structural motifs.
8. Some Common Protein Motifs:
β-hairpin.
β-meander.
Alpha-alpha corner.
Helix-turn-helix motif.
β-α-β motif.
β-sandwich.
β-barrel.
Greek key.
The Jellyroll topology.
Omega loop.
Zinc finger motif.
9. Conclusion.
10. References.
LEVELS OF PROTEIN STRUCTURE
This document discusses the different levels of protein structure, including primary, secondary, tertiary, and quaternary structure. It explains that proteins are made up of amino acids joined by peptide bonds to form polypeptide chains. The sequence of amino acids determines the protein's primary structure. Secondary structure involves folding of the polypeptide chain into structures like alpha helices and beta sheets. Tertiary structure describes how secondary structure elements interact spatially through interactions like hydrogen bonding and disulfide bridges to create the 3D structure of a protein. Quaternary structure refers to the way multiple polypeptide subunits combine and interact to form a functional protein complex. The document also outlines how understanding protein structure is important for structure-
Proteins.
Proteins are composed of amino acids and have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structure involves local folding into patterns like alpha helices and beta sheets. Tertiary structure is the overall three-dimensional shape formed by interactions between different parts of the polypeptide chain. Quaternary structure refers to the shape of proteins with multiple polypeptide subunits. Proteins perform many important functions in the body as enzymes, antibodies, hormones, and structural components.
Protein metabolism and nitrogen fixation and metabolism
- The document discusses protein metabolism and nitrogen fixation. It covers the classification of proteins based on their structure, composition, and functions. There are four levels of protein structure - primary, secondary, tertiary, and quaternary.
- The primary structure is the linear sequence of amino acids. The secondary structure involves folding into alpha helices or beta sheets via hydrogen bonding. Tertiary structure describes the overall 3D shape formed by interactions between amino acid R groups. Quaternary structure applies to proteins with multiple polypeptide chains that combine to form complexes.
- Proteins are classified as globular, fibrous, or intermediate based on their shape. They can also be simple or conjugated based on composition
Phys 02 13
There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids in the polypeptide chain. The secondary structure involves hydrogen bonds forming coils, sheets, or loops. Tertiary structure is the packing of these secondary structures into domains. Quaternary structure involves multiple proteins combining. A protein's shape determines its function, and denaturation can destroy this shape and impair function.
Protein & their Biochemical Role part 3
This document discusses proteins, their structure and functions. It covers the following key points:
1. Proteins are made of amino acids bonded together by peptide bonds. Their structure involves primary, secondary, tertiary and sometimes quaternary levels. Secondary structure includes alpha helices and beta sheets formed by hydrogen bonding.
2. Proteins have many important biochemical roles such as enzymes, hormones, antibodies, and structural components. Diseases can result from protein deficiencies or metabolic disorders affecting amino acid breakdown.
3. Protein structure can be disrupted through denaturation which unfolds secondary and tertiary levels, though the primary structure is maintained. Some examples of related diseases include phenylketonuria and maple syrup urine
proteins and its classification
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.
Protein Folding
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.
Protein stability
Proteins are polymers made of amino acids that carry out essential functions in organisms. They have primary, secondary, tertiary, and quaternary levels of structure determined by amino acid sequence and interactions. Stability depends on factors like temperature, pH, and solvents. Proteins misfold due to mutations or environmental stresses but normally fold into functional native states guided by energy landscapes. Functions include storage, transport, defense, cell signaling, and more. Purification techniques separate proteins from cell lysates using techniques like extraction, precipitation, chromatography. Determination methods identify proteins using X-ray crystallography or NMR spectroscopy.
Protein structure
Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structures include alpha helices and beta sheets formed by hydrogen bonding of the polypeptide chain. Tertiary structure refers to the overall three-dimensional shape that results from interactions between amino acid side chains. Quaternary structure involves interactions between multiple protein subunits.
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This document provides an overview of protein structure and folding. It discusses the four levels of protein structure - primary, secondary, tertiary, and quaternary. Common secondary structures like alpha helices and beta sheets are described. The document also introduces concepts like the Ramachandran plot, which maps allowed phi and psi dihedral angles in protein backbones. Protein folding and factors involved like molecular chaperones are also summarized. Disorders resulting from changes in protein conformation are briefly mentioned.
Lec 2 level 3-de(chemistry of proteins)
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.pptx
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.
Structure and classifications of proteins
This document discusses the structure and classifications of proteins. It describes the primary, secondary, tertiary, and quaternary structures of proteins. The primary structure is the linear sequence of amino acids. Secondary structures include alpha-helices and beta-sheets formed by hydrogen bonding between amino acids. Tertiary structure refers to the 3D conformation of the entire polypeptide chain. Quaternary structure involves interactions between multiple polypeptide subunits. The document also classifies proteins based on their function, composition/solubility, and nutritional levels. Common protein structures and several color reaction tests for identifying proteins are outlined.
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The document discusses protein and peptides, including their structure and stability problems. It describes the primary, secondary, tertiary, and quaternary structure of proteins. Issues like denaturation, adsorption, aggregation, and precipitation are explained as stability problems for proteins and peptides. The conclusion emphasizes the need for viable delivery systems to efficiently deliver proteins and peptides in biologically active forms through non-parenteral routes.
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- 1. PROTEINS Dr.Kavitha.S.Kumar Assistant Professor Department of Biochemistry St. Mary’s College Thrissur-680020 Kerala
- 2. Proteins,Dr.Kavitha.S.Kumar,St.Mary’s College Proteins are biochemical compounds consisting of one or more polypeptides typically folded into a globular or fibrous form in a biologically functional way Proteins are made of 20 amino acids linked by peptide bonds Polypeptide backbone is the repeating sequence of the N-C-C-N-C- C… in the peptide bond The side chain or R group is not part of the backbone or the peptide bond
- 4. Proteins,Dr.Kavitha.S.Kumar,St.Mary’s College Protein Folding The peptide bond allows for rotation around it and therefore the protein can fold and orient the R groups in favorable positions Weak non-covalent interactions will hold the protein in its functional shape – these are the shape Non-covalent Bonds in Proteins
- 5. Proteins,Dr.Kavitha.S.Kumar,St.Mary’s College Hydrogen Bonds in Proteins H-bonds form between 1. atoms involved in the peptide bond 2. peptide bond atoms and R groups 3. R groups
- 6. Proteins,Dr.Kavitha.S.Kumar,St.Mary’s College Protein Folding Proteins shape is determined by the sequence of the amino acids The final shape is called the conformation and has the lowest free energy possible Denaturation is the process of unfolding the protein Can be down with heat, pH or chemical compounds In the chemical compound, can remove and have the protein renature or refold
- 7. Proteins,Dr.Kavitha.S.Kumar,St.Mary’s College Levels of Organization 1. Primary structure Amino acid sequence of the protein 2. Secondary structure H bonds in the peptide chain backbone -helix and -sheets 3. Tertiary structure Non-covalent interactions between the R groups within the protein 4. Quanternary structure Interaction between 2 polypeptide chains
- 9. Proteins,Dr.Kavitha.S.Kumar,St.Mary’s College Globular Proteins – most of what we have dealt with so far Compact shape like a ball with irregular surfaces Enzymes are globular Fibrous Proteins – usually span a long distance in the cell 3-D structure is usually long and rod shaped Types of Proteins