structure, properties and biological functions of proteins.
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The primary structure of a protein is its amino acid sequence. It has an N-terminal end with a free NH3+ group and a C-terminal end with a free COO- group. The secondary structure involves hydrogen bonding between amino acids and forms alpha helices, beta pleated sheets, or triple helices. The tertiary structure is the overall 3D shape from interactions between amino acid side chains far apart in the sequence. Quaternary structure refers to the association of multiple polypeptide chains in an oligomeric protein.
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Four levels of protein structure
A comprehensive presentation on Four levels of protein structure for MBBS, BDS, B Pharm & Biotechnology students to facilitate self- study.
PROTEIN STRUCTURE PRESENTATION
The document discusses the structure of proteins at various levels of organization:
- Proteins are composed of amino acids linked together by peptide bonds to form polypeptide chains. The sequence and interactions of these chains determine the protein's structure.
- There are four levels of protein structure - primary, secondary, tertiary, and quaternary. Secondary structure includes alpha helices and beta sheets formed by hydrogen bonding between amino acids in the chain. Tertiary structure describes the overall 3D shape formed by interactions between amino acid side chains. Quaternary structure involves the interaction of multiple polypeptide chains.
- Protein structure enables proteins to perform their diverse functions through processes like enzyme catalysis, oxygen transport, and providing structure
Chemiosmotic Theory
A Remarkable Conflict Between Biochemical Dogma And Radical Concept :
Traditional Concept :
By the 1950s it had been clearly established that oxidative phosphorylation involved the stepwise transfer of electrons through a series of carriers to molecular oxygen. But how the energy derived from these electron transfer reactions was converted to ATP remained a mystery. The general assumption was that ADP was converted to ATP by direct transfer of high-energy phosphate groups from some other intermediate. Thus it was postulated that high-energy intermediates were produced as a result of electron transfer reactions and that these intermediates drove ATP synthesis by phosphate group transfer.
Concept Proposed By Peter Mitchell :
The fundamental proposal of the chemiosmotic hypothesis was that the โintermediateโ that coupled electron transport to ATP synthesis was a proton electrochemical gradient across the membrane. Mitchell postulated that such a gradient was produced by electron transport and that the flow of protons back across the membrane in the energetically favorable direction was then coupled to ATP synthesis
Structural level of organization of proteins
description of different levels of structural organization of proteins and renaturation and denaturation of proteins
Structural organisation of protiens
Proteins are polymers of amino acids joined by peptide bonds. They have four levels of structural organization: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structures include alpha helices and beta sheets. Tertiary structure refers to the overall 3D shape of a protein formed by interactions between residues. Quaternary structure involves interactions between multiple polypeptide subunits. Examples like myoglobin, hemoglobin, and collagen illustrate these different structural levels.
Protein structure
- Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids in the polypeptide chain. Secondary structure involves hydrogen bonding that forms alpha helices and beta sheets. Tertiary structure is the 3D shape formed by interactions between different parts of the polypeptide. Quaternary structure refers to the assembly of multiple polypeptide subunits.
Structure of protiens and the applied aspects
The slides explain the structures of proteins, the bond stabilizing the structure of amino acids, the different types of protein structures, the applied aspects and the newer advances in the protein structure.
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.
Recommended
Four levels of protein structure
A comprehensive presentation on Four levels of protein structure for MBBS, BDS, B Pharm & Biotechnology students to facilitate self- study.
PROTEIN STRUCTURE PRESENTATION
The document discusses the structure of proteins at various levels of organization:
- Proteins are composed of amino acids linked together by peptide bonds to form polypeptide chains. The sequence and interactions of these chains determine the protein's structure.
- There are four levels of protein structure - primary, secondary, tertiary, and quaternary. Secondary structure includes alpha helices and beta sheets formed by hydrogen bonding between amino acids in the chain. Tertiary structure describes the overall 3D shape formed by interactions between amino acid side chains. Quaternary structure involves the interaction of multiple polypeptide chains.
- Protein structure enables proteins to perform their diverse functions through processes like enzyme catalysis, oxygen transport, and providing structure
Chemiosmotic Theory
A Remarkable Conflict Between Biochemical Dogma And Radical Concept :
Traditional Concept :
By the 1950s it had been clearly established that oxidative phosphorylation involved the stepwise transfer of electrons through a series of carriers to molecular oxygen. But how the energy derived from these electron transfer reactions was converted to ATP remained a mystery. The general assumption was that ADP was converted to ATP by direct transfer of high-energy phosphate groups from some other intermediate. Thus it was postulated that high-energy intermediates were produced as a result of electron transfer reactions and that these intermediates drove ATP synthesis by phosphate group transfer.
Concept Proposed By Peter Mitchell :
The fundamental proposal of the chemiosmotic hypothesis was that the โintermediateโ that coupled electron transport to ATP synthesis was a proton electrochemical gradient across the membrane. Mitchell postulated that such a gradient was produced by electron transport and that the flow of protons back across the membrane in the energetically favorable direction was then coupled to ATP synthesis
Structural level of organization of proteins
description of different levels of structural organization of proteins and renaturation and denaturation of proteins
Structural organisation of protiens
Proteins are polymers of amino acids joined by peptide bonds. They have four levels of structural organization: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structures include alpha helices and beta sheets. Tertiary structure refers to the overall 3D shape of a protein formed by interactions between residues. Quaternary structure involves interactions between multiple polypeptide subunits. Examples like myoglobin, hemoglobin, and collagen illustrate these different structural levels.
Protein structure
- Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids in the polypeptide chain. Secondary structure involves hydrogen bonding that forms alpha helices and beta sheets. Tertiary structure is the 3D shape formed by interactions between different parts of the polypeptide. Quaternary structure refers to the assembly of multiple polypeptide subunits.
Structure of protiens and the applied aspects
The slides explain the structures of proteins, the bond stabilizing the structure of amino acids, the different types of protein structures, the applied aspects and the newer advances in the protein structure.
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.
Quaternary structure of protein
Quaternary structure refers to the arrangement of multiple protein subunits into a single protein complex. Hemoglobin is a common example that is made of two alpha and two beta subunits. The subunits interact through hydrophobic interactions, hydrogen bonding, and other bonds. Globular proteins tend to have quaternary structure that clusters the subunits into a spherical shape, while fibrous proteins form long coils or sheets through interactions between subunits. Quaternary structure allows proteins to take on specialized functions beyond what individual subunits could achieve alone.
Protein structure & function
Proteins have a variety of functions in cells including enzymes, structural components, transporters, motors, and signaling molecules. A protein's unique 3D shape, determined by its amino acid sequence, allows it to carry out its specific function. The polypeptide backbone forms secondary structures like alpha helices and beta sheets. Non-covalent interactions further guide protein folding into a stable tertiary structure. Quaternary structure involves interactions between multiple polypeptide chains. Post-translational modifications and ligand binding regulate protein activity.
Amino acids
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.
Regulation of enzyme activity
1. Enzyme activity can be regulated through several mechanisms including allosteric regulation, feedback inhibition, proenzymes, and protein modification.
2. Allosteric enzymes have effector molecules that bind and induce a conformational change that increases or decreases enzyme activity. Feedback inhibition occurs when a metabolic end product inhibits an earlier enzyme.
3. Proenzymes are inactive precursors that are activated by proteolytic cleavage. Protein modification like phosphorylation can also regulate enzymes by changing their structure.
Secondary Structure Of Protein (Repeating structure of protein)
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.
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PROPERTIES OF AMINOACIDS.pptx
Amino acids are colorless, crystalline solids that have high melting points above 200 degrees Celsius. They are soluble in water and slightly soluble in alcohols. Amino acids are optically active and can form peptide bonds between their amino and carboxyl groups. They have zwitterionic and amphoteric properties due to possessing both amine and carboxylic acid functional groups. Common tests to identify amino acids include the ninhydrin, xanthoproteic, and reactions with reagents like nitrous acid or Sanger's reagent. The 20 standard amino acids are essential for building proteins and sustaining human health through roles like hormone production, muscle structure, and organ function.
Structure of proteins
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Protein structural organisation
Proteins play key roles in living systems through catalysis, transport, and information transfer. They have a hierarchical structure including primary, secondary, tertiary, and quaternary levels. The primary structure is the amino acid sequence, and higher levels of organization are determined by the primary structure. Protein folding and interactions between residues determine the final 3D tertiary and quaternary structures, which are critical for protein function. Misfolded proteins can cause diseases.
Ramachandran plot
The document discusses the Ramachandran plot, which shows statistically probable combinations of the phi and psi backbone torsion angles in proteins. It describes how these two angles describe rotations around bonds in the polypeptide backbone and influence protein folding. The plot reveals allowed and disallowed regions based on steric clashes between atoms at different angle combinations. Common structures like alpha helices and beta sheets correspond to allowed regions in the plot.
Structure of amino acids
Amino acids are the building blocks of proteins. They contain carboxyl and amino groups on the same carbon atom, which allows them to act as both acids and bases and take on a zwitterion structure with opposite charges. Amino acids are named using either a three letter code based on the first three letters of the amino acid name or a one letter code. Except for glycine, all amino acids have a chiral carbon and exist in the L-isomeric form. Amino acids can be classified based on their variable R groups as nonpolar, polar uncharged, aromatic, positively charged, or negatively charged.
Proteins
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.
Protein structure: details
This document discusses the different levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure refers to the amino acid sequence. Secondary structure includes alpha helices, beta sheets, and beta turns formed by hydrogen bonding between amino acids. Tertiary structure is the 3D conformation determined by interactions between side chains. Quaternary structure refers to the arrangement of multiple polypeptide subunits in multimeric proteins. The structures are determined through techniques like X-ray crystallography and NMR.
Lipid200 structure and function
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Purine and Pyrimidine biosynthesis
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Classification and properties of protein
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Enzyme specificity
Enzymes exhibit specificity in their catalytic activity. The active site of an enzyme precisely binds substrates through weak interactions. The active site contains catalytic groups that directly participate in bond breaking and forming. Specificity depends on the atomic configuration of the active site. The lock-and-key model describes the active site as rigidly binding one substrate shape. However, the induced fit model is more accurate, with a flexible active site that adjusts its shape to substrates to improve catalysis. Enzyme specificity can be relative to bond type, moderate based on substrate structural groups, absolute to one substrate, or dual to multiple substrates through one or two reaction types.
Determination of primary structure of proteins
The document discusses the determination of the primary structure of proteins. It begins by explaining that proteins are composed of amino acid residues linked by peptide bonds to form a polypeptide chain. The primary structure refers to the specific sequence of amino acids in this chain. Mass spectrometry and tandem mass spectrometry techniques are used to analyze protein fragments obtained through enzymatic or chemical cleavage to determine the amino acid sequence and thereby elucidate the primary structure.
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Supersecondary structure ppt
The document discusses various supersecondary structures of proteins, which are intermediate structures between secondary and tertiary protein structures. It describes several common motifs composed of two or more secondary structures, such as helix-turn-helix, helix-loop-helix, beta-hairpins, and the Rossmann fold. These motifs are building blocks that occur frequently in protein structures and are associated with specific functions like DNA binding. The document provides detailed examples and diagrams of different supersecondary structure motifs involving helices, strands, and their combinations.
Protein; its functions
Protein is composed of amino acids linked together in chains. It is essential for life and is contained in every part of the body. There are two main types of protein - fibrous proteins found in animals that serve structural functions, and globular proteins that usually do not have structural roles and can be enzymes or transporters. Protein has critical physiological functions including building, maintaining, and repairing body tissues, and can also be converted to energy when intake is greater than requirements. The structure of proteins involves four levels - primary, secondary, tertiary, and quaternary.
Protein structure
Proteins are composed of amino acids bonded together in chains called polypeptides. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the sequence of amino acids in the polypeptide chain. The secondary structure describes local folding patterns like alpha helices and beta sheets formed by hydrogen bonds. Tertiary structure refers to the overall 3D shape formed by interactions between amino acids distant in the chain. Quaternary structure involves the interaction of multiple polypeptide chains. Changes in protein structure can alter its function.
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Quaternary structure of protein
Quaternary structure refers to the arrangement of multiple protein subunits into a single protein complex. Hemoglobin is a common example that is made of two alpha and two beta subunits. The subunits interact through hydrophobic interactions, hydrogen bonding, and other bonds. Globular proteins tend to have quaternary structure that clusters the subunits into a spherical shape, while fibrous proteins form long coils or sheets through interactions between subunits. Quaternary structure allows proteins to take on specialized functions beyond what individual subunits could achieve alone.
Protein structure & function
Proteins have a variety of functions in cells including enzymes, structural components, transporters, motors, and signaling molecules. A protein's unique 3D shape, determined by its amino acid sequence, allows it to carry out its specific function. The polypeptide backbone forms secondary structures like alpha helices and beta sheets. Non-covalent interactions further guide protein folding into a stable tertiary structure. Quaternary structure involves interactions between multiple polypeptide chains. Post-translational modifications and ligand binding regulate protein activity.
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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.
Regulation of enzyme activity
1. Enzyme activity can be regulated through several mechanisms including allosteric regulation, feedback inhibition, proenzymes, and protein modification.
2. Allosteric enzymes have effector molecules that bind and induce a conformational change that increases or decreases enzyme activity. Feedback inhibition occurs when a metabolic end product inhibits an earlier enzyme.
3. Proenzymes are inactive precursors that are activated by proteolytic cleavage. Protein modification like phosphorylation can also regulate enzymes by changing their structure.
Secondary Structure Of Protein (Repeating structure of protein)
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.
Centrioles (introduction, function, duplication )
Centrioles are cytoplasmic organelles found in eukaryotic cells that lack a limiting membrane or DNA. They are composed mainly of tubulin protein and arranged in a 9+3 pattern of microtubules. Centrioles help organize microtubules and form basal bodies for cilia/flagella. During cell division, the centrioles move to opposite poles and form the mitotic spindle, helping pull sister chromatids apart into daughter cells. Centrioles duplicate during S phase and are involved in both mitosis and meiosis.
PROPERTIES OF AMINOACIDS.pptx
Amino acids are colorless, crystalline solids that have high melting points above 200 degrees Celsius. They are soluble in water and slightly soluble in alcohols. Amino acids are optically active and can form peptide bonds between their amino and carboxyl groups. They have zwitterionic and amphoteric properties due to possessing both amine and carboxylic acid functional groups. Common tests to identify amino acids include the ninhydrin, xanthoproteic, and reactions with reagents like nitrous acid or Sanger's reagent. The 20 standard amino acids are essential for building proteins and sustaining human health through roles like hormone production, muscle structure, and organ function.
Structure of proteins
Gives in detail primary, secondary, tertiary and Quaternary structure of proteins. Gives classification of secondary structure: alpha helix, beta pleated sheet and different types of tight turns and explains most commonly found tight turn in proteins i.e. beta turn. Briefs about the Ramachandran plot of proteins, dihedral or torsion angles and explains why glycine and proline act as alpha helix breakers. Explains tertiary structure of proteins and different covalent and non covalent bonds in the tertiary structure and relative importance of these bonding interactions. Details about the quaternary structure of proteins and explains why hemoglobin is a quaternary protein and insulin is not.
Protein structural organisation
Proteins play key roles in living systems through catalysis, transport, and information transfer. They have a hierarchical structure including primary, secondary, tertiary, and quaternary levels. The primary structure is the amino acid sequence, and higher levels of organization are determined by the primary structure. Protein folding and interactions between residues determine the final 3D tertiary and quaternary structures, which are critical for protein function. Misfolded proteins can cause diseases.
Ramachandran plot
The document discusses the Ramachandran plot, which shows statistically probable combinations of the phi and psi backbone torsion angles in proteins. It describes how these two angles describe rotations around bonds in the polypeptide backbone and influence protein folding. The plot reveals allowed and disallowed regions based on steric clashes between atoms at different angle combinations. Common structures like alpha helices and beta sheets correspond to allowed regions in the plot.
Structure of amino acids
Amino acids are the building blocks of proteins. They contain carboxyl and amino groups on the same carbon atom, which allows them to act as both acids and bases and take on a zwitterion structure with opposite charges. Amino acids are named using either a three letter code based on the first three letters of the amino acid name or a one letter code. Except for glycine, all amino acids have a chiral carbon and exist in the L-isomeric form. Amino acids can be classified based on their variable R groups as nonpolar, polar uncharged, aromatic, positively charged, or negatively charged.
Proteins
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.
Protein structure: details
This document discusses the different levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure refers to the amino acid sequence. Secondary structure includes alpha helices, beta sheets, and beta turns formed by hydrogen bonding between amino acids. Tertiary structure is the 3D conformation determined by interactions between side chains. Quaternary structure refers to the arrangement of multiple polypeptide subunits in multimeric proteins. The structures are determined through techniques like X-ray crystallography and NMR.
Lipid200 structure and function
Lipids are a diverse group of compounds that are insoluble in water but soluble in organic solvents. They include fats, oils, waxes, sterols, and phospholipids. The document discusses the structure, function, and classification of various lipids. It describes simple lipids like triglycerides and waxes, as well as complex lipids including phospholipids. Phospholipids are important structural components of cell membranes and contain a phosphate group, alcohol, and fatty acids. Glycerophospholipids are the major class of phospholipids, with phosphatidylcholine, phosphatidylethanolamine, and others playing important roles in cells and tissues.
Purine and Pyrimidine biosynthesis
Nucleotide Biosynthesis involves 2 processes. one is Denovo synthesis and other is Salvage pathway. An outline of both the processes has given in this presentation.
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.
Enzyme specificity
Enzymes exhibit specificity in their catalytic activity. The active site of an enzyme precisely binds substrates through weak interactions. The active site contains catalytic groups that directly participate in bond breaking and forming. Specificity depends on the atomic configuration of the active site. The lock-and-key model describes the active site as rigidly binding one substrate shape. However, the induced fit model is more accurate, with a flexible active site that adjusts its shape to substrates to improve catalysis. Enzyme specificity can be relative to bond type, moderate based on substrate structural groups, absolute to one substrate, or dual to multiple substrates through one or two reaction types.
Determination of primary structure of proteins
The document discusses the determination of the primary structure of proteins. It begins by explaining that proteins are composed of amino acid residues linked by peptide bonds to form a polypeptide chain. The primary structure refers to the specific sequence of amino acids in this chain. Mass spectrometry and tandem mass spectrometry techniques are used to analyze protein fragments obtained through enzymatic or chemical cleavage to determine the amino acid sequence and thereby elucidate the primary structure.
Biosynthesis of amino acids
This document summarizes the biosynthesis of amino acids from key metabolic precursors. It discusses 6 families of amino acid biosynthesis defined by their precursor: (1) ฮฑ-ketoglutarate family (glutamate, glutamine, proline, arginine), (2) 3-phosphoglycerate family (serine, glycine, cysteine), (3) oxaloacetate family (aspartate, asparagine, methionine, threonine, lysine), (4) pyruvate family (alanine, valine, leucine, isoleucine), (5) phosphoenolpyruvate and erythrose 4-phosphate family (tryptoph
Supersecondary structure ppt
The document discusses various supersecondary structures of proteins, which are intermediate structures between secondary and tertiary protein structures. It describes several common motifs composed of two or more secondary structures, such as helix-turn-helix, helix-loop-helix, beta-hairpins, and the Rossmann fold. These motifs are building blocks that occur frequently in protein structures and are associated with specific functions like DNA binding. The document provides detailed examples and diagrams of different supersecondary structure motifs involving helices, strands, and their combinations.
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Protein; its functions
Protein is composed of amino acids linked together in chains. It is essential for life and is contained in every part of the body. There are two main types of protein - fibrous proteins found in animals that serve structural functions, and globular proteins that usually do not have structural roles and can be enzymes or transporters. Protein has critical physiological functions including building, maintaining, and repairing body tissues, and can also be converted to energy when intake is greater than requirements. The structure of proteins involves four levels - primary, secondary, tertiary, and quaternary.
Protein structure
Proteins are composed of amino acids bonded together in chains called polypeptides. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the sequence of amino acids in the polypeptide chain. The secondary structure describes local folding patterns like alpha helices and beta sheets formed by hydrogen bonds. Tertiary structure refers to the overall 3D shape formed by interactions between amino acids distant in the chain. Quaternary structure involves the interaction of multiple polypeptide chains. Changes in protein structure can alter its function.
Protein Structure and Function
The document discusses protein structure and function. It describes the basic building blocks of proteins, amino acids, and how they combine to form the primary structure. It then explains how the primary structure can take on regular patterns called secondary structures, including alpha helices and beta sheets. Alpha helices form coiled structures stabilized by hydrogen bonds between amino acids, while beta sheets involve hydrogen bonding between peptide chains to form extended structures. The precise sequence and folding of a protein's amino acids determines its final three-dimensional shape and function.
Nucleic Acids Structure and Functions
1. The document outlines the structure and function of nucleic acids DNA and RNA.
2. Key points covered include the central dogma of molecular biology, the Watson-Crick structure of DNA, types of RNA like mRNA, tRNA and rRNA, and their roles in gene expression and protein synthesis.
3. The document also discusses properties of nucleic acids like denaturation and reannealing of DNA as well as unique features of eukaryotic mRNA.
Protein structure classification
This document discusses protein structure, classification, prediction, and visualization. It covers secondary structure elements like alpha helices and beta sheets, as well as tertiary and quaternary structure. It describes protein structure databases like the Protein Data Bank and tools for visualizing protein structures. Different amino acid properties that influence secondary structure are also discussed.
PROTEINS
This document discusses proteins, including their definition, composition, sources, storage, requirements, functions, structure, and classification. Some key points:
- Proteins are polypeptides composed of amino acids joined by peptide bonds. They are essential to life and perform many catalytic, structural, transport, and other functions.
- Sources of proteins include animal sources like meat and dairy as well as plant sources like legumes. Storage capacity in organisms is limited compared to carbohydrates and fats.
- Proteins are classified based on their nutritional value, function, structure, and physicochemical properties. Complete proteins contain all essential amino acids while incomplete proteins lack some.
- Structure depends on shape - globular
Proteins biochemistry
Proteins are composed of amino acids that link together via peptide bonds. There are 20 naturally occurring amino acids that vary in properties like polarity, charge, and ability to form secondary structures. The sequence and interactions of amino acids give proteins their unique 3D structures and functions. Denaturation disrupts non-covalent bonds within proteins, altering their shapes and eliminating biological activity.
Protein structure
Describes the structural organisation of proteins with example and its determination, interrelationship b/w structure and function of proteins, also biologically important peptides is covered.
by Dr. N. Sivaranjani, MD
Urea cycle
The urea cycle is a series of biochemical reactions that occur primarily in the liver to convert excess ammonia into urea for excretion. The cycle involves the condensation of ammonia with carbon dioxide to form carbamoyl phosphate, followed by a series of reactions to add the carbamoyl group to various nitrogen-containing compounds to eventually form urea. Urea is then transported to the kidneys and excreted in urine to remove toxic ammonia from the body. The cycle requires energy in the form of ATP and occurs through five enzyme-catalyzed steps to synthesize urea from ammonia and carbon dioxide.
Nucleic acids
DNA and RNA are nucleic acids that store and help express genetic information. DNA is composed of nucleotides containing deoxyribose, phosphates, and one of four nitrogenous bases (adenine, guanine, cytosine, thymine). RNA is similar but contains ribose and uracil instead of thymine. The genetic code is stored in DNA as base pair sequences in chromosomes. During cell division, DNA replicates and genes direct protein production through transcription of DNA to mRNA and translation of mRNA to proteins.
Protein classification
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
Protein Powerpoint
The document discusses the structure and formation of proteins. It explains that amino acids join through condensation reactions to form peptide bonds, releasing a water molecule. Multiple peptide bonds form polypeptide chains of varying lengths that fold into unique 3D shapes to serve as functional proteins, such as structural, storage, transport, hormonal, receptor, contractile, defensive, and enzymatic proteins. Common food sources of protein are also mentioned.
Protein Structure & Function
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.
Protein
Proteins are composed of amino acids and play many essential roles in the body. They have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence, secondary involves hydrogen bonding into shapes like alpha helices and beta sheets, tertiary is the 3D folding of these structures, and quaternary involves the assembly of multiple protein subunits. Proteins serve as enzymes, hormones, antibodies, and structures. They undergo synthesis from amino acids and breakdown through catabolism. Disorders can occur if amino acid metabolism is disrupted.
Proteins slides
Proteins are made of amino acids and their structure and function are determined by their sequence and folding. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. Enzymes are proteins that catalyze biochemical reactions and examples include hydrolases and lactase. The structure and function of enzymes can be affected by factors like temperature, pH, and inhibitors. An enzyme lab was described that extracts the enzyme tyrosinase from mushrooms to test its reaction rate under normal and altered conditions.
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Similar to structure, properties and biological functions of proteins.
10879264.ppt
1) A protein's structure is determined by its amino acid sequence and consists of four levels: primary, secondary, tertiary, and quaternary.
2) The two most common secondary structures are alpha helices and beta sheets, which are stabilized by hydrogen bonds between amino acids.
3) Tertiary structure describes the overall 3D shape of a protein formed by interactions between regions of the polypeptide chain distant in primary sequence. Quaternary structure involves interactions between multiple protein subunits.
Proteins Structure
Proteins are the most abundant organic molecules in living systems, making up about 50% of cellular dry weight. They occur throughout the cell and form the basic structure and functions of life. All proteins are polymers of amino acids. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids joined by peptide bonds. Secondary structure involves hydrogen bonding that causes regions of the polypeptide chain to fold into alpha helices or beta sheets. Tertiary structure describes the three-dimensional shape that proteins fold into. Quaternary structure refers to complexes of multiple polypeptide subunits.
PROTEINS.pdf
There are four levels of protein structure:
1) Primary structure is the linear sequence of amino acids linked by peptide bonds. The specific sequence determines a protein's unique properties.
2) Secondary structure involves hydrogen bonding between amino acids that form regular patterns like alpha helices and beta sheets. Alpha helices have amino acids bonded in a spiral pattern while beta sheets have amino acids bonded side-by-side.
3) Tertiary structure is the overall 3D shape of a protein determined by interactions between R groups of amino acids.
4) Quaternary structure involves the spatial relationships between multiple protein subunits that combine through non-covalent bonds to carry out functions.
Week 3- Protein Folding and Structure.pdf
Protein structure is hierarchical, proceeding from primary to quaternary structure. Primary structure refers to the linear sequence of amino acids. Secondary structure involves folding into alpha helices and beta sheets. Tertiary structure describes the overall three-dimensional shape of a polypeptide. Quaternary structure refers to the arrangement of multiple protein subunits. Several methods can determine protein structure at high resolution, including X-ray crystallography, NMR spectroscopy, cryo-electron microscopy, and X-ray free electron lasers.
Protein structure
Protein structure can be described at several levels of organization. The primary structure is the amino acid sequence, while the secondary structure describes local patterns like alpha helices and beta sheets formed by hydrogen bonds. Tertiary structure refers to the overall 3D shape of a single polypeptide chain. Quaternary structure involves the arrangement of multiple protein subunits. Together these organizational levels allow proteins to carry out their diverse functions in the cell.
Protein strucutre prediction
This document discusses protein structure prediction through computational tools. It begins by stating that determining a protein's 3D structure from its amino acid sequence is a key challenge, and that experimental methods cannot keep up with the pace of genomic sequencing. It then provides an overview of the different levels of protein structural hierarchy that computational tools can predict, from the starting amino acid sequence to predicted 3D models. The document also outlines the primary, secondary, tertiary, and quaternary levels of protein structure.
Strutural organisation of proteins
The document discusses the four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids in the peptide chain. The secondary structure involves hydrogen bonding that causes the chain to fold into structures like alpha helices or beta sheets. Tertiary structure describes further folding and interactions that result in the protein's three-dimensional shape. Quaternary structure refers to multiple peptide chains linked together in a protein.
Protein structure basics
The document summarizes key aspects of protein structure and function. It discusses the building blocks of proteins, amino acids, and how they combine through peptide bonds to form protein primary structures. It then describes the four levels of protein structure - primary, secondary, tertiary, and quaternary - focusing on common secondary structures like alpha helices and beta sheets, and how their packing forms tertiary and quaternary structures. Experimental methods for determining protein structures like X-ray crystallography and NMR are also summarized.
Pengetahuan struktur, bentuk dan sintesa protein
The document discusses the four levels of protein structure: primary, secondary, tertiary, and quaternary. It explains that proteins are made of amino acids that are linked together via peptide bonds. The order and sequence of amino acids determines the primary structure. Hydrogen bonding leads to the formation of regular structures like alpha helices and beta sheets, which make up the secondary structure. Tertiary structure refers to the overall three-dimensional shape of the protein, which is stabilized by interactions between amino acid side chains. Some proteins have quaternary structure consisting of multiple polypeptide subunits.
structureofproteins-161119045143.pptx
The document describes the four levels of protein structure:
1) Primary structure is the linear sequence of amino acids joined by peptide bonds.
2) Secondary structure involves localized patterns like alpha helices and beta sheets formed by hydrogen bonds.
3) Tertiary structure is the overall 3D shape of the polypeptide chain formed by interactions like disulfide bridges, hydrogen bonds, and hydrophobic interactions.
4) Quaternary structure refers to complexes of multiple polypeptide subunits.
Protein structure
Proteins are polymers made up of amino acid chains that form specific structures. There are four levels of protein structure:
1. Primary structure is the amino acid sequence.
2. Secondary structures include alpha helices and beta sheets formed by hydrogen bonds between amino acids.
3. Tertiary structure is the three dimensional folding of secondary structures.
4. Quaternary structure occurs in proteins made of multiple polypeptide chains that aggregate. The document discusses these levels of structure in detail, focusing on alpha helices and beta sheets as common secondary structures stabilized by hydrogen bonding.
Secondary structure of proteins
The document summarizes key aspects of secondary protein structure, including the two main types - alpha helix and beta pleated sheet. It describes the alpha helix as a right-handed spiral stabilized by hydrogen bonds between amino acids four positions apart in the sequence. The beta pleated sheet involves hydrogen bonding between adjacent protein molecules in a zigzag pattern. Both secondary structures are important for determining the 3D shape of globular proteins. The Ramachandran plot is also introduced as a way to visualize allowed backbone dihedral angles in protein structures.
Proteins
Proteins are made up of chains of amino acids that form various structures which determine the protein's function. The amino acid sequence forms the primary structure. Hydrogen bonding forms regular patterns of alpha helices and beta sheets as the secondary structure. Tertiary structure is the final 3D shape from hydrophobic interactions. Some proteins have quaternary structure as complexes of multiple polypeptide chains.
Proteins
Proteins are made up of chains of amino acids that form various structures which determine the protein's function. The amino acid sequence forms the primary structure. Hydrogen bonding forms regular patterns of alpha helices and beta sheets as the secondary structure. Tertiary structure is the final 3D shape from hydrophobic interactions. Some proteins have quaternary structure as complexes of multiple polypeptide chains.
Protein
The document discusses various topics related to protein structure and function. It defines different types of bonds in proteins including peptide bonds, disulfide bonds, and hydrogen bonds. It describes the 20 common amino acids that make up proteins and different secondary structures such as alpha helices and beta sheets. It discusses the four levels of protein structure - primary, secondary, tertiary, and quaternary structure. It also covers protein folding driven by hydrophobic interactions and hydrogen bonding, as well as denaturation of proteins.
Secondary structure of proteins- Sonal Singh Shrivas.pptx
Proteins are complex molecules made up of long chains of amino acids. The secondary structure of a protein refers to the local folding patterns that occur within these chains. The two most common types of secondary structures are alpha helices and beta sheets.
In an alpha helix, the polypeptide chain is coiled in a right-handed spiral, with hydrogen bonds forming between the carbonyl oxygen of one amino acid and the amide hydrogen of an amino acid three residues down the chain. This structure gives the alpha helix a rod-like shape, which is stabilized by these hydrogen bonds.
In contrast, beta sheets consist of extended strands of amino acids that are held together by hydrogen bonds between adjacent strands. These strands can be either parallel, with the amino acids in each strand oriented in the same direction, or antiparallel, with the amino acids in each strand oriented in opposite directions. Beta sheets can form flat, sheet-like structures, or can be twisted to form a more compact structure.
Other secondary structures, such as beta turns and loops, also play important roles in protein structure and function. These structures help to stabilize the overall three-dimensional shape of the protein, which is critical for its function.
Proteins.pdf
Proteins are polypeptide structures made up of one or more extended chains of residues from the amino acid. They provide a wide range of organism tasks, including as DNA replication, molecule transport, metabolic process catalysis, and cell structural support.
The albumins seen in vast quantities in egg whites typically have a distinct 3D structure as a result of bonds that form between the proteinโs various amino acids. These bonds are broken by heating, exposing the hydrophobic (water-hating) amino acids that are typically maintained on the inside of the protein 1, 1 comma, 2 end superscript, 2, start superscript. In an effort to escape the water that surrounds them in the egg white, the hydrophobic amino acids will bind to one another, creating a protein network that gives the egg white structure and makes it white and opaque. Ta-da! Protein denaturation, thank you for another wonderful breakfast
Amino acids and protein
Amino acids are organic compounds containing amino and carboxylic acid groups. There are about 300 amino acids in nature but only 20 are found in proteins. Amino acids are linked together via peptide bonds to form polypeptide chains and proteins. There are four levels of protein structure - primary, secondary, tertiary, and quaternary - that determine a protein's shape and function. Proteins can be classified as simple proteins which break down into amino acids, or conjugated proteins which break down into a protein and non-protein component like lipids or carbohydrates.
Proteins by Salman Saeed Lecturer Botany UCMS Khanewal
This document discusses proteins and their structure and function. It begins by introducing proteins as polymers made of amino acids linked into peptide chains. It then covers the 20 main amino acids, how they are classified, and how peptide bonds form. It describes the primary, secondary, tertiary, and quaternary structural organization of proteins. Specific proteins discussed include hemoglobin, which transports oxygen in our blood, and myoglobin, which stores oxygen in muscles.
Similar to structure, properties and biological functions of proteins. (20)
Secondary structure of proteins- Sonal Singh Shrivas.pptx
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Proteins by Salman Saeed Lecturer Botany UCMS Khanewal
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asexual and-sexual_reproduction
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04 implantation (1)
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structure, properties and biological functions of proteins.
- 1. Primary structure of ะฐ protein โข The primary structure of ะฐ protein is the sequence of amino acids present in its peptide chain or chains. โข The end with the free H3 N+ group is called the N-terminal end, and the end with the free ะกะะ- group is called the ะก- terminal end.
- 3. Secondary structure of ะฐ protein โข The secondary structure of ะฐ protein is the arrangement in space of the atoms in the backbone of the protein. Three major types of protein secondary structure are known; the alpha helix, the beta pleated sheet, and the triple helix. The major force responsible for all three types of secondary structure is hydrogen bonding between ะฐ carbonyl oxygen atom of ะฐ peptide linkage and the hydrogen atom of an amino group (-NH) of another peptide linkage farther along the backbone.
- 5. Alpha Helix โข The Alpha Helix The alpha helix (ฮฑ-helix) structure resembles ะฐ coiled helical spring, with the coil configuration maintained by hydrogen bonds between N โ ะ and ะก= ะ groups of every fourth amino acid
- 6. Beta pleated sheet โข The beta pleated sheet (ฮฒ-pleated sheet) secondary structure involves amino acid chains that are almost completely extended. ย
- 7. Tertiary structure The tertiary structure of ะฐ protein is the overall three-dimensional shape that results from the attractive forces between amino acid side chains (R groups) that are widely separated from each other within the chain. There are four types of bonding interactions between "side chains" including: hydrogen bonding, salt bridges, disulfide bonds, and non-polar hydrophobic interactions.
- 10. Quaternary structure โข Quaternary structure is the highest level of protein organization. It is found only in proteins that have structures involving two or more polypeptide chains that are independent of each other โ that is, are not covalently bonded to each other. These multichain proteins are often called oligomeric proteins. The quaternary structure of ะฐ protein involves the associations among the separate chains in an oligomeric protein.
- 11. Hemoglobin