STRUCTURAL ORGANIZATION OF PROTEINS
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Primary structure of protein Secondary structure of protein Tertiary structure of protein Quaternary structure of protein Methods to determine protein structure Conclusion References METHODS TO DETERMINE PROTEIN STRUCTURE Each protein has a unique sequence of amino acids. The amino acids are held together in a protein by covalent peptide bonds or linkages. A peptide bond are formed when amino group of an amino acid combines with the carboxyl group of another. The conformation of polypeptide chain by twisting or folding is referred to as secondary structure. Two types of secondary structures α-helix and β-sheet are mainly identified. α-Helical structure was proposed by Pauling and Corey in 1951. It occurs when the sequence of amino acids are linked by hydrogen bonds. Each turn of α-helix contains 3.6 amino acids. β-pleated sheets are composed of two or more segments of fully extended peptide chains. β-Sheets may be arranged either in parallel or anti-parallel direction. Many globular proteins contain combinations of α-helix and β-pleated sheet secondary structure, these patterns are called supersecondary structures also called motifs. The three dimensional arrangement of protein structure is referred to as tertiary structure. It is a compact structure with hydrophobic side chains held interior while the hydrophilic groups are on the surface. This type of arrangement provide stability of the molecule. Besides the H-bongs, disulfide bonds, ionic interactions, hydrophobic interactions also contribute to the tertiary structure.
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Phospholipids
This document discusses phospholipids and their subclasses. Phospholipids contain fatty acids, phosphoric acid, and nitrogenous bases or alcohols. The two main classes are glycerophospholipids, containing glycerol, and sphingophospholipids, containing sphingosine. Lecithin and cephalin are important glycerophospholipids. Phospholipids form cell membranes and regulate permeability. They also participate in fat absorption and transport and removal of cholesterol from the body. The document also briefly discusses glycolipids, lipoproteins, steroids like cholesterol, and their structure and functions.
PYRUVATE DEHYDROGENASE COMPLEX (PDH-MULTI-ENZYME COMPLEX)
Pyruvate is converted to acetyl CoA by the pyruvate dehydrogenase (PDH) complex in the mitochondria. PDH is a multi-enzyme complex containing five coenzymes and three enzymes that catalyzes the oxidative decarboxylation of pyruvate. This generates acetyl CoA, NADH, and FADH2, with the NADH and FADH2 contributing to ATP production through oxidative phosphorylation. PDH activity is regulated by phosphorylation/dephosphorylation and end-product inhibition by acetyl CoA and NADH.
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
Heteropolysaccharide
Introduction
Definition
Classification of polysaccharides
1- Homopolysaccharides
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Type of heteropolysaccharides
Function of heteropolysaccharides
Conclusion
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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.
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Glycolysis
Metabolic pathways can be catabolic, involving the breakdown of complexes, or anabolic, involving synthesis. Glycolysis is the catabolic pathway that breaks down glucose into pyruvate, producing a net yield of 2 ATP per glucose molecule. It occurs in two phases: the preparatory phase requires 2 ATP to phosphorylate and cleave glucose, while the payoff phase generates 4 ATP from substrate-level phosphorylation as the intermediates are oxidized to pyruvate. Overall, glycolysis oxidizes glucose to pyruvate, reduces NAD+ to NADH, and generates a small amount of ATP through substrate-level phosphorylation.
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PYRUVATE DEHYDROGENASE COMPLEX (PDH-MULTI-ENZYME COMPLEX)
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Conclusion
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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.
Beta-oxidation of fatty acids
This document provides information on beta-oxidation of fatty acids. It discusses the three stages of beta-oxidation: activation of fatty acids in the cytosol, transport into mitochondria via carnitine shuttle, and beta-oxidation in the mitochondrial matrix. The four reactions of each beta-oxidation cycle are also described: oxidation, hydration, oxidation, and cleavage. Deficiencies in beta-oxidation can cause conditions like sudden infant death syndrome.
Glycolysis
Metabolic pathways can be catabolic, involving the breakdown of complexes, or anabolic, involving synthesis. Glycolysis is the catabolic pathway that breaks down glucose into pyruvate, producing a net yield of 2 ATP per glucose molecule. It occurs in two phases: the preparatory phase requires 2 ATP to phosphorylate and cleave glucose, while the payoff phase generates 4 ATP from substrate-level phosphorylation as the intermediates are oxidized to pyruvate. Overall, glycolysis oxidizes glucose to pyruvate, reduces NAD+ to NADH, and generates a small amount of ATP through substrate-level phosphorylation.
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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.
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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.
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1) The de novo pathway synthesizes purine nucleotides from simple precursors through a two-stage process forming IMP and then converting it to AMP or GMP.
2) The salvage pathway recycles purine bases and nucleosides obtained from the diet or cell turnover to form nucleotides.
3) Both pathways work together to synthesize the purine nucleotides needed for nucleic acid synthesis, with the salvage pathway playing a larger role in certain tissues.
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TCA CYCLE
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GLYCOLYSIS & ITS REGULATION
Glycolysis is the metabolic pathway that converts glucose into pyruvate, generating a small amount of ATP. It occurs in the cytosol of cells and has three phases: energy investment, splitting of molecules, and energy generation. Glycolysis is regulated by three key enzymes - hexokinase, phosphofructokinase, and pyruvate kinase. It yields two ATP per glucose under anaerobic conditions when pyruvate is reduced to lactate, and eight ATP when pyruvate enters the citric acid cycle under aerobic conditions.
Classification of protein
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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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Polysaccharides types and Structural Features
1. The document discusses types and structural features of polysaccharides. It describes homopolysaccharides like starch, dextrin, inulin, glycogen, and cellulose.
2. Starch is composed of amylose and amylopectin subunits linked by alpha-glucosidic bonds. Dextrin is formed from starch hydrolysis and has a similar structure to amylopectin.
3. Inulin is a polymer of fructose typically with a terminal glucose. Glycogen stores glucose in animals and has highly branched alpha-linked subunits. Cellulose, the main component of plant cell walls, is composed of beta-glucose units.
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.
Protein structures by amina
Proteins have four levels of structure:
1) Primary structure is the linear sequence of amino acids in the polypeptide chain held together by peptide bonds.
2) Secondary structure involves the local 3D structure of portions of the chain, forming alpha helices or beta sheets.
3) Tertiary structure describes the overall 3D structure of a single polypeptide chain, including side chains.
4) Quaternary structure refers to the 3D arrangement of multiple polypeptide subunits that make up a single protein.
Proteins 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.
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TCA CYCLE & ITS REGULATION
The TCA cycle, also known as the Krebs cycle or citric acid cycle, is the central metabolic pathway that catalyzes the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins to produce carbon dioxide, water, and energy in the form of ATP, NADH, and FADH2. The TCA cycle occurs in the mitochondrial matrix and is the final common pathway for the oxidation of these three macronutrient types. Through a series of chemical reactions, acetyl-CoA is oxidized, producing carbon dioxide and hydrogen ions that will be used in the electron transport chain to generate ATP through oxidative phosphorylation.
Gluconeogenesis -
Gluconeogenesis is the formation of glucose from non-carbohydrate precursors and occurs primarily in the liver and kidneys. Key substrates include lactate, glycerol, and glucogenic amino acids. The process is regulated by substrate availability and key enzymes such as pyruvate carboxylase and phosphoenolpyruvate carboxykinase. Gluconeogenesis is critical for maintaining blood glucose levels during periods of fasting or low carbohydrate intake.
classification of Amino acids
Amino acids are organic compounds that contain amine, carboxyl, and side chain groups. There are over 500 known amino acids, though only 20 are used in proteins. Amino acids can be classified in several ways, including by their side chain properties, polarity, distribution in proteins, and nutritional requirements. Some key classifications include nonpolar amino acids with aliphatic or aromatic side chains, polar but uncharged amino acids, and negatively or positively charged amino acids. Essential amino acids cannot be synthesized by the human body and must come from dietary sources, while nonessential amino acids can be synthesized. Amino acid classification provides a framework for understanding their structures and properties.
Genetic code
The genetic code is a dictionary that translates nucleotide sequences into amino acid sequences. It is composed of 64 codons that are read in groups of three nucleotides. The genetic code is universal, unambiguous, redundant, and non-overlapping. It specifies 20 standard amino acids through 61 codons, while 3 codons are stop signals that terminate protein synthesis. The code allows for wobbling in base pairing at the third position of codons, increasing decoding efficiency. Mutations can alter protein sequences through changes to codons.
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.
Globular and fibrous proteins
This document summarizes and provides examples of two main types of proteins: fibrous proteins and globular proteins. Fibrous proteins have little tertiary structure and form long fibers or sheets through cross-linkages of parallel polypeptide chains. They are usually insoluble and structural, such as keratin and collagen. Globular proteins have complex 3D structures that are folded into spherical shapes. They are usually soluble and play roles in metabolic reactions as enzymes and hemoglobin. Hemoglobin and collagen are provided as examples, with hemoglobin being globular and oxygen-carrying, while collagen is fibrous and structural in skin, bones and other tissues.
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
De novo and salvage pathway of purines
Jayati Mishra presented on the de novo and salvage pathways of purines under the guidance of Pradip Hirapue. The presentation discussed:
1) The de novo pathway synthesizes purine nucleotides from simple precursors through a two-stage process forming IMP and then converting it to AMP or GMP.
2) The salvage pathway recycles purine bases and nucleosides obtained from the diet or cell turnover to form nucleotides.
3) Both pathways work together to synthesize the purine nucleotides needed for nucleic acid synthesis, with the salvage pathway playing a larger role in certain tissues.
Glycolipid ppt
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HMP SHUNT PATHWAY
The HMP shunt, also known as the pentose phosphate pathway or phosphogluconate pathway, is an alternative pathway to glycolysis and the TCA cycle for glucose oxidation. It is more anabolic in nature and concerned with biosynthesis of NADPH and pentoses. Approximately 10% of glucose enters this pathway daily, with the liver and RBCs metabolizing around 30% of glucose through this pathway. The HMP shunt occurs in the cytosol and generates NADPH and pentoses like ribose-5-phosphate, which are important for lipid, steroid, and nucleic acid synthesis. No ATP is directly utilized or produced in the HMP shunt.
Amino acid
Amino acids are organic compounds that contain an amino group, a carboxyl group, a central carbon atom, and a side chain. There are 20 standard amino acids that are the building blocks of proteins. Amino acids can be classified based on their structure, polarity, nutritional requirements, and metabolic fate. They perform important functions including serving as monomers for protein synthesis, participating in cellular processes, and acting as precursors for other compounds.
TCA CYCLE
The tricarboxylic acid (TCA) cycle is a series of enzyme-catalyzed reactions that forms a key part of aerobic respiration in cells. It was discovered by Hans Krebs in 1937 and is also known as the Krebs cycle or citric acid cycle. The cycle occupies a central position in metabolism, using acetate to generate carbon dioxide, reducing agents like NADH, and ATP through oxidative phosphorylation. It provides precursors for amino acid and nucleotide biosynthesis. The cycle is critical for generating the majority of a cell's energy needs through the complete oxidation of carbohydrates, fatty acids, and amino acids.
Classification of lipids
This document provides an overview of lipid classification and functions. It discusses the main classes of lipids including fatty acids, triacylglycerols, phospholipids, glycolipids, lipoproteins, and steroids. Within each class, specific lipid types are defined along with their structures and functions. The document also briefly outlines some lipid metabolism disorders and the clinical significance of lipids.
GLYCOLYSIS & ITS REGULATION
Glycolysis is the metabolic pathway that converts glucose into pyruvate, generating a small amount of ATP. It occurs in the cytosol of cells and has three phases: energy investment, splitting of molecules, and energy generation. Glycolysis is regulated by three key enzymes - hexokinase, phosphofructokinase, and pyruvate kinase. It yields two ATP per glucose under anaerobic conditions when pyruvate is reduced to lactate, and eight ATP when pyruvate enters the citric acid cycle under aerobic conditions.
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.
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.
Transamination & deamination
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Lipids properties, classification, function
This document defines and describes various types of lipids. It begins by explaining that lipids are a heterogeneous group of compounds related to fatty acids, fats, oils, waxes and other substances. It then discusses the basic components of lipids like fatty acids, glycerol and their esters known as triglycerides. The document further classifies lipids into simple lipids, compound lipids and derived lipids. Various types of phospholipids, glycolipids, sterols and terpenoids are also explained. Physical and chemical properties of lipids are outlined along with their important functions in living organisms.
Polysaccharides types and Structural Features
1. The document discusses types and structural features of polysaccharides. It describes homopolysaccharides like starch, dextrin, inulin, glycogen, and cellulose.
2. Starch is composed of amylose and amylopectin subunits linked by alpha-glucosidic bonds. Dextrin is formed from starch hydrolysis and has a similar structure to amylopectin.
3. Inulin is a polymer of fructose typically with a terminal glucose. Glycogen stores glucose in animals and has highly branched alpha-linked subunits. Cellulose, the main component of plant cell walls, is composed of beta-glucose units.
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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3) Tertiary structure describes the overall 3D structure of a single polypeptide chain, including side chains.
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The document discusses protein structure and function. It begins by introducing proteins as linear polymers made of amino acids, with the specific sequence determined by DNA. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. Primary structure refers to the sequence of amino acids. Secondary structure involves regular conformations like coils and folds. Tertiary structure describes the three-dimensional structure of the whole protein. Quaternary structure involves interactions between multiple protein subunits in a complex. The document also lists the 20 common amino acids that make up proteins and provides references for further reading.
Biology form 4
The document discusses protein structure and function. It begins by introducing proteins as linear polymers made of amino acids, with the sequence specified by DNA. It then describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. Primary structure refers to the sequence of amino acids. Secondary structure involves regular conformations like coils and folds. Tertiary structure describes the 3D shape of the whole protein chain. Quaternary structure involves interactions between multiple protein subunits in a complex. The document also lists the 20 common amino acids and provides references for further reading.
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.
Structure of Protein
Proteins have four levels of structural organization: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids in the polypeptide chain. The secondary structure involves local folding into shapes like alpha helices and beta pleated sheets. Tertiary structure describes the overall three-dimensional shape of the protein, which depends on its function. Quaternary structure refers to the arrangement of multiple polypeptide subunits that make up some proteins. Understanding these levels of structure is important for comprehending a protein's role.
Harish
This document discusses the structure and properties of proteins. It begins with an introduction stating that proteins are polymers of amino acids and are involved in most body functions. It then discusses the primary, secondary, tertiary, and quaternary levels of protein structure. The primary structure is the amino acid sequence. Secondary structures include alpha helices and beta pleated sheets formed by hydrogen bonds. Tertiary structure is determined by interactions between amino acid side chains. Quaternary structure results from multiple polypeptide subunits aggregating. Proteins have various properties like solubility, molecular weight, and shape. They also have important functions like structure, enzymes, hormones, and more.
Structure Of Protein
– Primary structure
– Secondary structure
– Tertiary structure
– Quaternary structure
It consists of; β sheet, α-helix, β-pleated sheet, β-bends, Non repetitive structures, Super secondary structures.
SUPER SECONDARY STRUCTURES (MOTIFS):
5 - Proteins, hemoglobin & myoglobin.pptx
This document provides information about proteins presented in a biochemistry lecture. It defines proteins as macromolecules made of amino acid polymers. Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structures include alpha helices and beta sheets formed by hydrogen bonding. Tertiary structure involves protein folding into three-dimensional shapes. Quaternary structure involves interactions between protein subunits. Examples discussed are hemoglobin, which carries oxygen in red blood cells, and myoglobin, which stores oxygen in muscle cells. Both contain heme but hemoglobin transports oxygen while myoglobin stores it.
Introduction to protein engg
This document provides an introduction to protein structure and function. It discusses that proteins are made up of amino acids and have different levels of structure, including primary, secondary, tertiary, and sometimes quaternary structure. The primary structure is the amino acid sequence. Secondary structure includes alpha helices and beta sheets formed by hydrogen bonds. Tertiary structure refers to the overall shape of the folded polypeptide chain. Quaternary structure describes the arrangement of multiple polypeptide subunits in a single protein. Understanding these hierarchical levels of structure is important for determining a protein's function.
Proteins
Protein are the most abundant organic molecule of living systems. They occur in every part of the cell and constitutive about 50% of the cellular dry weight.Proteins form the fundamental basis of structure and functional unit of life. Unlike lipids and carbohydrates, proteins are not stored, so they must be consumed daily.
Current recommended daily intake for adults is 0.8 grams of protein per kg of body weight (more is needed for children). Dietary protein comes from eating meat and milk.
Architecture of proteins
Proteins are made up of amino acids joined together in chains that fold up into complex three-dimensional shapes determined by their primary, secondary, tertiary, and sometimes quaternary structure. There are 20 different amino acids that can be arranged in primary structures and then fold into secondary structures like alpha helices and beta sheets driven by hydrogen bonding. Tertiary structure describes how the whole chain folds into its final 3D shape through interactions between amino acid side chains. Some proteins have quaternary structure involving clustering of multiple chains.
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.
Similar to STRUCTURAL ORGANIZATION OF PROTEINS (20)
Protein metabolism and nitrogen fixation and metabolism
Protein metabolism and nitrogen fixation and metabolism
Proteins-Classification ,Structure of protein, properties and biological impo...
Proteins-Classification ,Structure of protein, properties and biological impo...
More from Shylesh M
Topological manupilation of DNA.pptx
The topology of DNA is defined by how the two complementary single strand are intertwined
DNA in a relax state usually assumes the B-Conformation with10.6 bp per turn
DNA is subjected to bends or opening of DNA over winding or unwinding, its base pair turn changes and the DNA is subjected to stress and strain
DNA Topology also encompasses super coiling
RNA – i PATHWAY
RNA interference [ RNAi] is a sequence mechanism , triggered by the introduction of ds RNA leading to mRNA degradation
It results in switching the targeted gene on and off at transcriptional or post transcriptional level3
The long double stranded RNAs enter a cellular pathway that is known as RNA interference pathway .
First ds RNAs get processed into 20-25 nucleotides small interfering RNAs [siRNAs] by an enzyme Dicer .
Small interfering RNAs assemble into RNA induced silencing complexes [RISCs] ,unwinding in the process.
The siRNAs strands subsequently guide the RISCs complementary RNA molecules , where they cleave and destroy the RNA .
Cleavage of RNA takes place near the middle of the region bound by siRNA strand .
This results into mRNA Degradation.
Gene knockdown
Double stranded RNA is synthesized with a sequence complementary to a gene of interest and introduced into a cell organism ,where it is recognized as exogenous genetic material and activates the RNAi pathway .
Using this mechanism, researchers can cause drastic decrease in the expresssion of targeted gene .
Since RNAi may not totally abolish expression of the gene , this technique is referred to as knockdown.
Morphology Of Viruses : Viruses, structure and characteristics
Viruses can be extremely simple in design, consisting of nuclei acid
surrounded by the protein coat as a capsid.
The capsid is composed of smaller protein components
referred to as capsomeres.
The capsid along with genome combination
is called a nucleocapsid.
The viruses can also posses additional components,
with most common being an additional membranous layer
that surrounds nucleocapsid called an envelope.
This envelope is actually acquired from the nuclear or
plasma membrane of the infected host cell and then
Modified with viral protein called peplomere.
A complete virus, with all the components needed for
host cell to cause infection is referred to as virions.
Viruses come in many shapes and sizes, but these are consistent
and distinct for each viral family.
The morphology of virus include size, shapes, genetic constituents,
and the nuclear envelope
An infective agent that typically consist of a nuclei acid molecule In protein coat, it is too small can not visible through naked eyes and even by light microscopy, and is able to multiply only within the living cells of a host.
These are about 100 times smaller than bacteria and can only be observed by electron microscope.
These are small obligate intracellular parasites, which Contain either a RNA or DNA genome surrounded by a protective, virus protein coat.
These are acellular, so they are neither prokaryotes nor eukaryotes because they lack the characters of living beings except the ability to replicate. And they infect all types of cells :- humans, animals, plants, bacteria, yeast, protozoa, etc.
VIRAL SIZE:-
These are much smaller than bacteria for a time
they were know as’filterable agents’ as they can pass through
filters that can hold back bacteria.
They can not be seen under light microscope hence
called as'ultramicroscopic‘. These viral particles seen in this
manner are know as ‘elementary bodies’.
The size ranges:- 5-300nanometer.
In recent years a number of viruses including mimivirus length of
virus up to 600nm,and Pandoravirus Ranges from 50-100nm
In length have been identified.
Most viruses vary in diameter from 250-400nm;the largest,
however measure about 500nm in diameter and are about 700-1,000nm in length.
Paramyxoviruses can be up to 14,000nm long, Rotavirus particles measures 76.5nm in diameter.
Viruses, VIRAL STRUCTURE, MORPHOLOGY
Glyoxylate cycle PATHWAYS REACTION
A series of metabolic reactions by which many different organism utilise fats for the synthesis of carbohydrate
Another Process Involving Glycolytic Enzymes and Metabolites
Anabolic metabolic pathway occurring in plants, and several
microorganisms , fungi not animals.
Occurs in glyoxysome
The enzymes common to the TCA cycle and the glyoxysomes are isoenzymes, one specific to mitochondria and the other to glyoxysomes.
The glyoxylate cycle allows plants to use acetyl-CoA derived from β-oxidation of fatty acids for carbohydrate synthesis (use fats for the synthesis of carbohydrates).
The glyoxylate cycle is a cyclic pathway that result in conversion of 2 carbon fragment of Acetyl CoA TO 4 carbon compound succinate then succinate is covert to oxaloacetate and then glucose involving the reaction of gluconeogenesis
VIRUSES CLASSIFICATION , LIFE CYCLE OF VIRUSES. CHARACTERISTICS OF VIRUSES
VIRUSES
LIFE CYCLE OF BACTERIOPHAGES
The word virus is derived from Latin word venom which means poisonous fluid that causes infection.
The branch of science that deals with the study of viruses is called Virology. It is the branch of Microbiology.
They show living characters inside the host and non living characters outside the host.
They contain either DNA or RNA as genetic material.
They have different size and shape. They cause diseases in plants, animals and micro-organisms .
Not cellular
Cannot carry on metabolic activities independently.
Contain either DNA or RNA, not both ( true cells contain both ).
Lack ribosomes and enzymes necessary for protein synthesis.
Reproduce only within cells they infect.
CLASSIFICATION OF VIRUSES
Holmes, in 1948, proposed a simple system of classifying viruses based on the type of cell (host) they infect:
Phytophagineae: They infect plants and they RNA as their genetic material. Eg: TMV,CaMV.
Zoophagineae: They infect animals and they have mostly DNA as their genetic material. Eg: Polio virus.
Pagineae: They infect bacterial cells, called bacteriophages they usually have DNA as genetic material.
Based on the viral envelope
Named after David Baltimore, a noble prize winning biologist n 1971.
1. dsDNA viruses Eg: Adenoviruses, Herpiviruses.
2. ssDNA viruses Eg: Paravoviruses.
3. dsRNA viruses Eg: Reoviruses.
4. (+)ssRNA viruses Eg: Picornaviruses.
5. (-)ssRNA viruses Eg: Orthomyxoviruses.
6. ssRNA-RT viruses Eg: Retroviruses.
7. dsDNA-RT viruses Eg: Hepadnaviruses.
Tobacco mosaic:
Causative agent: Tobacco mosaic virus (TMV)
Symptoms: The leaves of infected plants develop mosaic patches ,it is due to destruction of chlorophyll or due to production of abnormal chlorophyll .blisters appear in the region of dark green spots these may be regular or irregular in advanced stages leaves curl and get distorted.
Adsorption of the virion to the bacterial cell.
Penetration and decoating of the nucleic acid .
Protein synthesis.
Breakdown of bacterial DNA.
Arrest of host cell development.
Replication of phage DNA.
Maturation of infective progeny.
Lysis and release of newly formed phages.
Holmes, in 1948, proposed a simple system of classifying viruses based on the type of cell (host) they infect:
Phytophagineae: They infect plants and they RNA as their genetic material. Eg: TMV,CaMV.
Zoophagineae: They infect animals and they have mostly DNA as their genetic material. Eg: Polio virus.
Pagineae: They infect bacterial cells, called bacteriophages they usually have DNA as genetic material.
SDS- Polyacrylamide Gel Electrophoresis
SDS-Polyacrylamide Gel Electrophoresis
What is SDS?
Preparation of Gel
Process of SDS-PAGE
Visualization of protein bands
SDS-PAGE is differentiated into two systems.
*continuous sds-page
*discontinuous sds-page.
Polyacrylamide is used to form a gel, a matrix of a pores which allow the molecules migrate at different rates.
Negatively charged detergent sodium dodecyl sulfate.
Used to denature and linearize the proteins
Coated the proteins with negatively charged.
SDS-page is a technique that used to separate proteins according to their molecular size through the gel.
Proteins are unfolded and migrate from cathode to anode terminal at different rates.
Molecular weight is determined by compare the result with a standard curve of relative motility of standard proteins.
Visualizes the band under UV light.
Types of stains;
Coomassie Blue;
* Coomassie Brilliant Blue staining The Coomassie dyes R-250 and G-250 bind to proteins stoichiometrically through their sulfonic acid groups.
* . The interactions between dye and protein are Van der Waals and ionic. The sulfonic acid groups interact with positive amine groups. Therefore coomassie dye binds to wide range of proteins.
* Limited to ~100ng of protein.
Silver stain;
*most sensitive test
*detection limit 0.1-1.0ng of protein
The size of pores is determined by the concentration of acrylamide.
The higher the concentration, the smaller the size of pores.
Discontinuos sds-page consist of two different gels.
*stacking gel -4%of acrylamide
*separating gel-range from 5-15% of acrylamide.
SOLID WASTE AND MANAGEMENT BIO GAS PRODUCTION
Source And Management
Agriculture
Fisheries
Household
Commercial and Industry
MANAGEMENT :-
Storage
Collection
Transport and Handling
Recyling
Biogas production
Biogas production from biomass is an anaerobic process.
The anaerobic digestion is usually carried out by using are referred to as anaerobic digesters.
A digester may be made up of concrete bricks and cement or steel, usually built underground.
The digester has an inlet attached to a mixing tank feeding cow dung.
The methanogenic bacteria from another digester are also added with cow dung.
The digester is attached to a movable gas holding or storage tank with a gas outlet.
The used slurry comes out from the digester through an outlet. This can be used as a manure.
Process of Biogas production
By products of Sugar Industries
Molasses
Molasses is a viscous by product of refining sugarcane or sugar beets into sugar.
It contain solids, sucrose and reducing sugars.
Total sugar content is 45-55%. Hence it is a valuable raw material for the producton of many value added products.
India has the largest chemical industry in the world using sugarcane molasses to produce acetaldehyde, acetic acid, polyvinyl chloride, synthetic rubber etc.
Citric acid is produced easily from molasses by submerged fermentation.
Bagasse is the fibrous matter that remains after sugarcane stalks are crushed to extract their juice.
It is a dry pulpy residue left after the extraction of juice from sugarcane.
Bagasse is used as a biofuel and in manufacture of pulp and building materials.
Biochemical Evidence For dna As Genetic Material
Biochemical Evidence For dna As Genetic Material
What is genetic material The genetic information in all cell is stored in DNA ,Discovery of Transformation in Bacteria , The transforming principle is DNA , HERSHEY & CHASE (1952) EXPERIMENT WITH T2 BACTERIOPHAGE, Summary of Hershey & Chase (1952 ) experiment
PRIONS AND VIROIDS
PRIONS AND VIROIDS , Diseases caused by Prions General properties , REPLICATION OF VIROIDS , viorids is 2 types
Vitamine B1 Thaimine Pyrophosphate
This document summarizes information about vitamin B1 (thiamine) and its active coenzyme form, thiamine pyrophosphate (TPP). It discusses the history of thiamine discovery and its chemical structure. Thiamine is converted to TPP in the liver and intestinal mucosa by the enzyme thiamine pyrophosphokinase using ATP. TPP acts as a coenzyme, transferring aldehyde groups in metabolic reactions. Sources of thiamine are mentioned and a deficiency can cause beriberi. Functions include roles in growth, nervous system maintenance, and metabolism.
STAINING TECHNIQUES AND TYPES PROCEDURE.
This document discusses various staining techniques used in microscopy to visualize bacteria and other microscopic organisms. It describes different types of stains including simple stains that color all structures the same and differential stains that color different structures differently. Specific staining techniques are explained, including Gram staining to distinguish between Gram-positive and Gram-negative bacteria, acid-fast staining for mycobacteria, and endospore staining. The document provides details on procedures, requirements, and results for common staining methods.
Capture of carbondioxide , entrapement of Co2
This document summarizes a seminar presentation on carbon dioxide (CO2) capture. It discusses how CO2 emissions have rapidly increased due to population growth and energy consumption. There are three main options to reduce CO2 emissions: improving energy efficiency, switching to non-fossil fuel energy sources, and developing carbon capture and storage (CCS) technologies. The document then describes the three main methods of CCS - pre-combustion, post-combustion, and oxyfuel combustion. It also discusses transporting the captured CO2 via pipelines and storing it underground through geo-sequestration in depleted oil fields, aquifers, and other rock formations. The advantages and disadvantages of CCS technologies are
FERMENTATION TYPES .
This document summarizes two main types of fermentation processes: solid state fermentation and submerged fermentation. Solid state fermentation occurs without free water and uses natural raw materials like grains as the carbon source to cultivate microorganisms. Submerged fermentation uses a liquid substrate and is best for microbes that require high moisture. Both methods have various applications, with solid state fermentation used for producing enzymes, biopesticides, and in bioremediation, while submerged fermentation is common in industrial manufacturing.
HUMAN CHROMOSOMAL ABERRATIONS AND KARYOTYPE ANALYSIS.
Chromosomal aberrations refer to changes in chromosome structure or number. The document discusses various types of structural aberrations like deletions, duplications, inversions, and translocations, and numerical aberrations involving changes in ploidy. Karyotype analysis involves staining and arranging chromosomes to identify aberrations. Abnormal karyotypes can lead to diseases like Down syndrome, Patau syndrome, and Cri du chat syndrome. The normal human karyotype contains 22 pairs of autosomes and an XX or XY sex chromosome complement.
More from Shylesh M (14)
Morphology Of Viruses : Viruses, structure and characteristics
Morphology Of Viruses : Viruses, structure and characteristics
VIRUSES CLASSIFICATION , LIFE CYCLE OF VIRUSES. CHARACTERISTICS OF VIRUSES
VIRUSES CLASSIFICATION , LIFE CYCLE OF VIRUSES. CHARACTERISTICS OF VIRUSES
HUMAN CHROMOSOMAL ABERRATIONS AND KARYOTYPE ANALYSIS.
HUMAN CHROMOSOMAL ABERRATIONS AND KARYOTYPE ANALYSIS.
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8.Isolation of pure cultures and preservation of cultures.pdf
Isolation of pure culture, its various method.
Deep Software Variability and Frictionless Reproducibility
Deep Software Variability and Frictionless ReproducibilityUniversity of Rennes, INSA Rennes, Inria/IRISA, CNRS
The ability to recreate computational results with minimal effort and actionable metrics provides a solid foundation for scientific research and software development. When people can replicate an analysis at the touch of a button using open-source software, open data, and methods to assess and compare proposals, it significantly eases verification of results, engagement with a diverse range of contributors, and progress. However, we have yet to fully achieve this; there are still many sociotechnical frictions.
Inspired by David Donoho's vision, this talk aims to revisit the three crucial pillars of frictionless reproducibility (data sharing, code sharing, and competitive challenges) with the perspective of deep software variability.
Our observation is that multiple layers — hardware, operating systems, third-party libraries, software versions, input data, compile-time options, and parameters — are subject to variability that exacerbates frictions but is also essential for achieving robust, generalizable results and fostering innovation. I will first review the literature, providing evidence of how the complex variability interactions across these layers affect qualitative and quantitative software properties, thereby complicating the reproduction and replication of scientific studies in various fields.
I will then present some software engineering and AI techniques that can support the strategic exploration of variability spaces. These include the use of abstractions and models (e.g., feature models), sampling strategies (e.g., uniform, random), cost-effective measurements (e.g., incremental build of software configurations), and dimensionality reduction methods (e.g., transfer learning, feature selection, software debloating).
I will finally argue that deep variability is both the problem and solution of frictionless reproducibility, calling the software science community to develop new methods and tools to manage variability and foster reproducibility in software systems.
Exposé invité Journées Nationales du GDR GPL 2024
Sharlene Leurig - Enabling Onsite Water Use with Net Zero Water
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Presented at June 6-7 Texas Alliance of Groundwater Districts Business MeetingCompexometric titration/Chelatorphy titration/chelating titration
Classification
Metal ion ion indicators
Masking and demasking reagents
Estimation of Magnisium sulphate
Calcium gluconate
Complexometric Titration/ chelatometry titration/chelating titration, introduction, Types-
1.Direct Titration
2.Back Titration
3.Replacement Titration
4.Indirect Titration
Masking agent, Demasking agents
formation of complex
comparition between masking and demasking agents,
Indicators/Metal ion indicators/ Metallochromic indicators/pM indicators,
Visual Technique,PM indicators (metallochromic), Indicators of pH, Redox Indicators
Instrumental Techniques-Photometry
Potentiometry
Miscellaneous methods.
Complex titration with EDTA.
Travis Hills' Endeavors in Minnesota: Fostering Environmental and Economic Pr...
Travis Hills of Minnesota developed a method to convert waste into high-value dry fertilizer, significantly enriching soil quality. By providing farmers with a valuable resource derived from waste, Travis Hills helps enhance farm profitability while promoting environmental stewardship. Travis Hills' sustainable practices lead to cost savings and increased revenue for farmers by improving resource efficiency and reducing waste.
The binding of cosmological structures by massless topological defects
Assuming spherical symmetry and weak field, it is shown that if one solves the Poisson equation or the Einstein field
equations sourced by a topological defect, i.e. a singularity of a very specific form, the result is a localized gravitational
field capable of driving flat rotation (i.e. Keplerian circular orbits at a constant speed for all radii) of test masses on a thin
spherical shell without any underlying mass. Moreover, a large-scale structure which exploits this solution by assembling
concentrically a number of such topological defects can establish a flat stellar or galactic rotation curve, and can also deflect
light in the same manner as an equipotential (isothermal) sphere. Thus, the need for dark matter or modified gravity theory is
mitigated, at least in part.
Remote Sensing and Computational, Evolutionary, Supercomputing, and Intellige...
Remote Sensing and Computational, Evolutionary, Supercomputing, and Intellige...University of Maribor
Slides from talk:
Aleš Zamuda: Remote Sensing and Computational, Evolutionary, Supercomputing, and Intelligent Systems.
11th International Conference on Electrical, Electronics and Computer Engineering (IcETRAN), Niš, 3-6 June 2024
Inter-Society Networking Panel GRSS/MTT-S/CIS Panel Session: Promoting Connection and Cooperation
https://www.etran.rs/2024/en/home-english/Equivariant neural networks and representation theory
Or: Beyond linear.
Abstract: Equivariant neural networks are neural networks that incorporate symmetries. The nonlinear activation functions in these networks result in interesting nonlinear equivariant maps between simple representations, and motivate the key player of this talk: piecewise linear representation theory.
Disclaimer: No one is perfect, so please mind that there might be mistakes and typos.
dtubbenhauer@gmail.com
Corrected slides: dtubbenhauer.com/talks.html
EWOCS-I: The catalog of X-ray sources in Westerlund 1 from the Extended Weste...
Context. With a mass exceeding several 104 M⊙ and a rich and dense population of massive stars, supermassive young star clusters
represent the most massive star-forming environment that is dominated by the feedback from massive stars and gravitational interactions
among stars.
Aims. In this paper we present the Extended Westerlund 1 and 2 Open Clusters Survey (EWOCS) project, which aims to investigate
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The primary targets of this project are Westerlund 1 and 2, the closest supermassive star clusters to the Sun.
Methods. The project is based primarily on recent observations conducted with the Chandra and JWST observatories. Specifically,
the Chandra survey of Westerlund 1 consists of 36 new ACIS-I observations, nearly co-pointed, for a total exposure time of 1 Msec.
Additionally, we included 8 archival Chandra/ACIS-S observations. This paper presents the resulting catalog of X-ray sources within
and around Westerlund 1. Sources were detected by combining various existing methods, and photon extraction and source validation
were carried out using the ACIS-Extract software.
Results. The EWOCS X-ray catalog comprises 5963 validated sources out of the 9420 initially provided to ACIS-Extract, reaching a
photon flux threshold of approximately 2 × 10−8 photons cm−2
s
−1
. The X-ray sources exhibit a highly concentrated spatial distribution,
with 1075 sources located within the central 1 arcmin. We have successfully detected X-ray emissions from 126 out of the 166 known
massive stars of the cluster, and we have collected over 71 000 photons from the magnetar CXO J164710.20-455217.
Applied Science: Thermodynamics, Laws & Methodology.pdf
When I was asked to give a companion lecture in support of ‘The Philosophy of Science’ (https://shorturl.at/4pUXz) I decided not to walk through the detail of the many methodologies in order of use. Instead, I chose to employ a long standing, and ongoing, scientific development as an exemplar. And so, I chose the ever evolving story of Thermodynamics as a scientific investigation at its best.
Conducted over a period of >200 years, Thermodynamics R&D, and application, benefitted from the highest levels of professionalism, collaboration, and technical thoroughness. New layers of application, methodology, and practice were made possible by the progressive advance of technology. In turn, this has seen measurement and modelling accuracy continually improved at a micro and macro level.
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3D Hybrid PIC simulation of the plasma expansion (ISSS-14)
3D Particle-In-Cell (PIC) algorithm,
Plasma expansion in the dipole magnetic field.
ESR spectroscopy in liquid food and beverages.pptx
With increasing population, people need to rely on packaged food stuffs. Packaging of food materials requires the preservation of food. There are various methods for the treatment of food to preserve them and irradiation treatment of food is one of them. It is the most common and the most harmless method for the food preservation as it does not alter the necessary micronutrients of food materials. Although irradiated food doesn’t cause any harm to the human health but still the quality assessment of food is required to provide consumers with necessary information about the food. ESR spectroscopy is the most sophisticated way to investigate the quality of the food and the free radicals induced during the processing of the food. ESR spin trapping technique is useful for the detection of highly unstable radicals in the food. The antioxidant capability of liquid food and beverages in mainly performed by spin trapping technique.
Randomised Optimisation Algorithms in DAPHNE
Slides from talk:
Aleš Zamuda: Randomised Optimisation Algorithms in DAPHNE .
Austrian-Slovenian HPC Meeting 2024 – ASHPC24, Seeblickhotel Grundlsee in Austria, 10–13 June 2024
https://ashpc.eu/
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Phenomics assisted breeding in crop improvement
As the population is increasing and will reach about 9 billion upto 2050. Also due to climate change, it is difficult to meet the food requirement of such a large population. Facing the challenges presented by resource shortages, climate
change, and increasing global population, crop yield and quality need to be improved in a sustainable way over the coming decades. Genetic improvement by breeding is the best way to increase crop productivity. With the rapid progression of functional
genomics, an increasing number of crop genomes have been sequenced and dozens of genes influencing key agronomic traits have been identified. However, current genome sequence information has not been adequately exploited for understanding
the complex characteristics of multiple gene, owing to a lack of crop phenotypic data. Efficient, automatic, and accurate technologies and platforms that can capture phenotypic data that can
be linked to genomics information for crop improvement at all growth stages have become as important as genotyping. Thus,
high-throughput phenotyping has become the major bottleneck restricting crop breeding. Plant phenomics has been defined as the high-throughput, accurate acquisition and analysis of multi-dimensional phenotypes
during crop growing stages at the organism level, including the cell, tissue, organ, individual plant, plot, and field levels. With the rapid development of novel sensors, imaging technology,
and analysis methods, numerous infrastructure platforms have been developed for phenotyping.
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STRUCTURAL ORGANIZATION OF PROTEINS
- 1. STRUCTURAL ORGANIZATION OF PROTEIN
- 2. Introduction Primary structure of protein Secondary structure of protein Tertiary structure of protein Quaternary structure of protein Methods to determine protein structure Conclusion References
- 3. Proteins (Greek: Proteios ‘Holding the first place’) are the most abundant organic molecules of the living system. They constitute about 50% of the cellular dry weight. They are the polymers of Lα-amino acids. The structures of proteins can be divided into 4 levels of organization: Primary structure Secondary structure Tertiary structure Quaternary structure
- 4. Each protein has a unique sequence of amino acids. The amino acids are held together in a protein by covalent peptide bonds or linkages. A peptide bond are formed when amino group of an amino acid combines with the carboxyl group of another.
- 5. The conformation of polypeptide chain by twisting or folding is referred to as secondary structure. Two types of secondary structures α-helix and β-sheet are mainly identified. α-Helical structure was proposed by Pauling and Corey in 1951. It occurs when the sequence of amino acids are linked by hydrogen bonds. Each turn of α-helix contains 3.6 amino acids. β-pleated sheets are composed of two or more segments of fully extended peptide chains. β-Sheets may be arranged either in parallel or anti-parallel direction. Many globular proteins contain combinations of α-helix and β-pleated sheet secondary structure, these patterns are called supersecondary structures also called motifs.
- 6. Fig: Secondary structures of proteins Fig: Parallel and anti-parallel strands
- 7. The three dimensional arrangement of protein structure is referred to as tertiary structure. It is a compact structure with hydrophobic side chains held interior while the hydrophilic groups are on the surface. This type of arrangement provide stability of the molecule. Besides the H-bongs, disulfide bonds, ionic interactions, hydrophobic interactions also contribute to the tertiary structure.
- 8. Fig: Tertiary structure of protein showing bonds Fig: 3D structure of protein
- 9. Proteins consisting of two or more polypeptides which may be identical or unrelated, such proteins are termed as oligomers and possess quaternary structure. The individual polypeptide chains are known as monomers. The monomeric subunits are held together by H-bonds, hydrophobic interactions and ionic bonds. These proteins play a significant role in the regulation of metabolism and cellular functions. E.g., Hemoglobin.
- 10. Fig: Quaternary structure of protein Fig: Levels of protein organization
- 11. The first protein structure was determined by protein crystallography was of Myoglobin by Max Perutz and John Kendrew in 1962. Currently used techniques including X-ray crystallography, NMR spectroscopy and Electron microscopy. Fig: X-Ray Crystallography
- 12. Fig: NMR Spectroscopy Fig: Electron microscopy
- 13. Proteins are the most abundant organic molecules of life, performing structural and dynamic functions in the living cells. The dynamic functions of proteins are highly diversified such as enzymes, hormones, clotting factors, immunoglobulins, etc.
- 14. M.C. Michael, L.N. David; Principles of Biochemistry; 5th edi; P:92-138; W.H. Freeman and Company. U. Satyanarayan, U. Chakrapani; Biochemistry; 3rd edi; P:43-68; Books and allied (P) Ltd. K. Pranav, M. Usha; Life Sciences; 5th edi; P:12-20; Pathfinder Publication.