Evolutionary relationship between diverse protein with similar domain
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This document discusses protein domains and their evolutionary relationship between diverse proteins. Protein domains are conserved parts of a protein sequence that determine structure and function. Domains act as compact, independently folding modules that provide specific catalytic and binding sites and serve as building blocks for large protein assemblies. Domains are found across different proteins and have been adapted through evolution, with some folds favored over others as they represent stable arrangements. Bioinformatics approaches like the Protein Data Bank and CATH classify protein structures into families and domains to better understand evolutionary relationships and comparisons between proteins.
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The peptide bond joins amino acids in polypeptides and proteins. It has partial double bond character which makes it nearly planar. This rigidity reduces flexibility during protein folding. The peptide bond is usually in the trans configuration to reduce steric hindrance, though proline can be cis or trans due to its cyclic side chain.
Biochemistry - Ch4 protein structure , and function
This document discusses the structure of proteins at multiple levels. It explains that a protein's amino acid sequence determines its 3D structure, and its structure dictates its function. Noncovalent interactions like hydrogen bonds, hydrophobic interactions, and electrostatic interactions are important forces that stabilize a protein's native structure. The peptide bond is rigid and planar, limiting the possible conformations of the polypeptide backbone. Common secondary structures like alpha helices and beta sheets form due to favorable hydrogen bonding patterns between peptide bonds.
Biochemistry - Ch3 Amino Acids , Peptides , Protein
This document provides an overview of proteins, amino acids, and peptides. It discusses how proteins perform important biological functions like catalysis, transport, and structure. It describes how amino acids are the building blocks of proteins and the different classifications of amino acids. It also summarizes how peptides are formed from amino acids and some of their functions. The document explains techniques used to separate, purify, and analyze proteins like chromatography, electrophoresis, and spectroscopy.
Respiratory #2, Gas Transport - Physiology
1) Gas exchange occurs at the lungs between blood and air, and at tissues between blood and tissues, via simple diffusion down partial pressure gradients.
2) The alveolar-capillary membrane is where oxygen diffuses from alveoli into blood and carbon dioxide diffuses from blood into alveoli. Factors like membrane thickness, surface area, and gas solubility and molecular weight determine diffusion rates.
3) Oxygen is transported in blood bound to hemoglobin (98.5%) and dissolved (1.5%). The oxygen content is the total oxygen carried in blood, while the oxygen carrying capacity is the maximum amount of oxygen hemoglobin can carry when saturated. Percent hemoglobin saturation indicates how
Peptides
Peptides are short chains of amino acids linked by peptide bonds. They are distinguished from proteins by typically containing fewer than 50 amino acid units. Peptides are formed through condensation reactions between carboxyl and amino groups of separate amino acids, releasing a water molecule. Peptide bonds are rigid and planar, contributing to protein structure stability. Peptides serve many important biological functions and can be classified based on their production method, including through ribosomal translation, nonribosomal synthesis, and enzymatic digestion of proteins in foods. Bioactive peptides derived from food proteins can have beneficial effects like lowering blood pressure, cholesterol, and antimicrobial properties.
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.
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.
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.
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Biochemistry - Ch1 foundation of Biochem , ch2 water and aqueous solution
Biochemistry - Ch1 foundation of Biochem , ch2 water and aqueous solution
Biochemistry - Ch4 protein structure , and function
Biochemistry - Ch4 protein structure , and function
Biochemistry - Ch3 Amino Acids , Peptides , Protein
Biochemistry - Ch3 Amino Acids , Peptides , Protein
Similar to Evolutionary relationship between diverse protein with similar domain
Protein and protein Dystrophin
Dystrophin is a high molecular weight cytoskeletal protein that localizes to the cytoplasmic face of the sarcolemma. It has four domains - an actin binding domain, a central rod domain composed of spectrin-like repeats, a cysteine-rich domain, and a carboxy-terminal domain. Dystrophin forms the dystrophin-glycoprotein complex with other proteins like dystroglycans and sarcoglycans to connect the actin cytoskeleton to the extracellular matrix. Mutations in dystrophin cause Duchenne/Becker muscular dystrophy by disrupting this connection and leading to muscle degeneration.
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.
Proteins
This document discusses proteins and their structure and functions. It notes that proteins are composed of chains of amino acids and perform a variety of important functions in organisms, including catalyzing reactions and transporting molecules. It describes the primary, secondary, tertiary, and quaternary structure of proteins. Proteins are assembled through the translation of genetic codes and can be synthesized chemically in laboratories. The document outlines several key cellular functions of proteins and notes they are responsible for carrying out the instructions specified in genes.
Protein Folding.pdf
Protein folding is the physical process by which a polypeptide folds into its characteristic three-dimensional structure. Folding begins with interactions between amino acids that form regions of secondary structure, which then fold into a compact three-dimensional structure. For some proteins, folding requires assistance from molecular chaperones such as Hsp70 and chaperonins, which help prevent misfolding and aggregation. Misfolded proteins can lead to loss of function or formation of protein aggregates associated with diseases like cystic fibrosis and Alzheimer's.
Protein Folding
This document discusses protein structure and folding. It describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structure involves folding into alpha helices or beta sheets. Tertiary structure is the overall 3D shape formed by interactions between amino acid side chains. Quaternary structure refers to interactions between multiple polypeptide chains in a protein. The document also discusses protein folding, denaturation, and misfolding, noting that many neurodegenerative diseases are associated with misfolded protein aggregates.
Protein metabolism and nitrogen fixation and metabolism
- The document discusses protein metabolism and nitrogen fixation. It covers the classification of proteins based on their structure, composition, and functions. There are four levels of protein structure - primary, secondary, tertiary, and quaternary.
- The primary structure is the linear sequence of amino acids. The secondary structure involves folding into alpha helices or beta sheets via hydrogen bonding. Tertiary structure describes the overall 3D shape formed by interactions between amino acid R groups. Quaternary structure applies to proteins with multiple polypeptide chains that combine to form complexes.
- Proteins are classified as globular, fibrous, or intermediate based on their shape. They can also be simple or conjugated based on composition
Protein motif. by KK Sahu sir
Introduction:
Protein
Protein motif.
2. History:
3. A brief overview of protein structure.
4. The Structural Classification of Protein(SCOP):
All α.
All β
α/β
α+β
5.The super secondary structure.
6. Rules for formation of Protein Motifs.
7. Structural motifs.
8. Some Common Protein Motifs:
β-hairpin.
β-meander.
Alpha-alpha corner.
Helix-turn-helix motif.
β-α-β motif.
β-sandwich.
β-barrel.
Greek key.
The Jellyroll topology.
Omega loop.
Zinc finger motif.
9. Conclusion.
10. References.
presentation. (1).pptx
The document discusses tertiary and quaternary protein structures. It defines tertiary structure as the specific 3D shape of a protein based on interactions between amino acid side chains. Tertiary structure results from disulfide bonds, hydrophobic interactions, hydrogen bonds, ionic interactions, and Van der Waals forces. Quaternary structure refers to the assembly of multiple polypeptide subunits into a single functional protein. Protein folding and molecular chaperones facilitate proper tertiary and quaternary structure formation.
Aug 26 2011
The document discusses several key topics regarding proteins and enzymes:
1. It describes the primary structure of proteins and how their amino acid sequence determines their function. It also discusses polymorphic proteins and early protein sequencing methods.
2. Protein folding and the factors that influence a protein's three-dimensional structure are summarized, including non-covalent bonds, domains, and common structural motifs like alpha helices and beta sheets.
3. The roles of different protein types like globular, fibrous, and assembly proteins are highlighted. Key fibrous proteins like collagen and elastin are also mentioned.
Biological roles of proteins
Proteins play very significant role in cell functioning. they are known as workhorse of cell. they are made up of amino acids.
7.5 proteins2
The document discusses the four levels of protein structure - primary, secondary, tertiary, and quaternary. It explains the significance of each level. The primary structure is the sequence of amino acids. The secondary structure involves hydrogen bonding that forms alpha helices and beta sheets. Tertiary structure describes the overall 3D shape formed by interactions between secondary structures. Quaternary structure refers to complexes of multiple polypeptide chains. The document also discusses membrane proteins and the roles of polar and non-polar amino acids in protein structure and function.
Proteins structure and role in gene expression
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 folding of the polypeptide into a compact 3D structure. Quaternary structure involves the assembly of multiple polypeptide subunits. Proteins play important roles in gene expression, with mRNA carrying the code from DNA to the ribosome for protein synthesis via translation of codons to amino acids. Regulation of transcription and translation allows cells to control and adapt protein production.
Protein structures by anivjeh
tertiary and quaternary structures of protein molecules
how long chain of amino acids (polypeptide) gets converted in to protein molecules
BT631-8-Folds_proteins
There are three main points about the relationship between protein structure and function:
1. Most proteins that share the same fold are evolutionarily related and perform similar functions. However, there are some examples where proteins with very different sequences adopt the same fold.
2. While some folds are associated with certain functions like binding specific ligands, the same fold can facilitate different biological functions. Individual residues, rather than the overall fold, often determine a protein's exact enzymatic activity.
3. There are examples of proteins that perform the same function but have totally different structures and evolved the same catalytic mechanism independently, showing functional convergence is possible.
Protein Chemistry and Functions
This document provides information on the structure and properties of proteins. It discusses the four levels of protein structure - primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structures include alpha helices and beta sheets. Tertiary structure involves the folding of the polypeptide chain. Quaternary structure involves the assembly of multiple polypeptide subunits. Proteins are classified by function, structure, composition, and nutritional value. Proteins play many important roles in the human body and are used in various applications.
Proteins
Proteins are composed of chains of amino acids and have four levels of structure: primary, secondary, tertiary, and quaternary. They perform many critical functions in the body as enzymes, hormones, antibodies, and structural components. Proteins can be classified based on their shape as globular or fibrous proteins, and based on their structural complexity as simple, conjugated, or derived proteins. They carry out roles in structures, functions, regulations, and protections in cells and tissues throughout the body.
report
Molecular chaperones play an important role in protein folding and preventing misfolding. The document discusses protein folding mechanisms and the roles of chaperones like GroEL/GroES complex. It summarizes protein folding, mechanisms of proteostasis including chaperones and quality control systems that help maintain protein homeostasis. The GroEL/GroES chaperone system is described in detail with its mechanism of encapsulating proteins to allow folding in an ATP-dependent manner.
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.
Proteins
The document discusses the basic structure and functions of proteins. Proteins are made up of amino acids that are linked together via peptide bonds. The primary structure is the sequence of amino acids, while secondary structure involves folding into alpha helices or beta sheets via hydrogen bonds. Tertiary structure refers to the overall 3D shape, which is important for a protein's function and is maintained by bonds and interactions between amino acids. There are two main types of protein structures - globular proteins that are compact and soluble, and fibrous proteins that form insoluble fibers. A change in a single amino acid can alter tertiary structure and affect a protein's function.
Protein: structure, classification,function and assay methods
definition , alpha helix beta pleated sheets tertiary and quarternary structure , peptide bond protein classification , assay methods, rhuemanns purple
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Protein metabolism and nitrogen fixation and metabolism
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Evolutionary relationship between diverse protein with similar domain
- 1. Evolutionary Relationship between Diverse Protein with similar Domain By: Rishabh Paliwal B100980BT
- 2. What is Domain? stable units of Protein. conserved part of a given protein sequence. decides structure and function of Protein. folded 3-D compact structure with stability. length vary between 25 to 500 amino acid.
- 3. Example Zinc finger with metal ion or disulfide bridges. functional domain like calcium-binding EF hand domain in calmodulin.
- 4. Domains in Protein Compact structural domain are found in diverse Protein. Independent folding. Naturally multifunctional and multidomains. Provides specific catalytic and binding sites. Serves modules for building up large assemblies.
- 5. Example pyruvate kinase to regulate F-6-P to pyruvate. contains 1. All β regulatory domain 2. An α/β substrate binding domain 3. An α/β nucleotide domain same as enzyme.
- 6. Evolution modules new sequences are adapted from pre-existing sequence. domains as modules. C and N terminal become close during evolution Found in all form of life. repetition of domain in diverse protein
- 7. Continue…. found among cell surface, cytokinin receptor, extracellular protein and matrix. molecular evolution in similar sequence and structure. some folds may be favored than others as they represent stable arrangements of secondary structures and some proteins may converge towards these folds over the course of evolution.
- 8. Bioinformatics Approach Protein Data Bank Deposited more than 90,000 experimentally determined protein structure. Various Set of similar structure. Classified in families to understand evolutionary relationship and comparison. Algorithm for assigned domain with 3-D structure
- 9. Continue…. CATH Has 800 fold families Super-fold families with at least three populated without significant sequence similarity. Most populated is α/β barrel super-fold