Built from 20 kinds of amino acids Each Protein has a three dimensional structure. Majority of...
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![Page 1: Built from 20 kinds of amino acids Each Protein has a three dimensional structure. Majority of proteins are compact. Highly convoluted molecules.](https://reader035.fdocuments.in/reader035/viewer/2022062408/56649e7e5503460f94b80cb0/html5/thumbnails/1.jpg)
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![Page 3: Built from 20 kinds of amino acids Each Protein has a three dimensional structure. Majority of proteins are compact. Highly convoluted molecules.](https://reader035.fdocuments.in/reader035/viewer/2022062408/56649e7e5503460f94b80cb0/html5/thumbnails/3.jpg)
Built from 20 kinds of amino acids
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Each Protein has a three dimensional structure.
Majority of proteins are compact. Highly convoluted molecules. Proteins are folded polypeptides. There are four levels of organization.
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What is a Protein Fold?
Compact, folding arrangement of the polypeptide chain
Chain folds to optimise packing of the hydrophobic residues in the interior core of the protein
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1. Primary structure ◦Amino acids joined by peptide bonds form a linear polypeptide chain
2. Secondary structure◦Polypeptide chains form sheets and coils
3. Tertiary structure◦Sheets and coils pack into functional domains
4. Quaternary structure__2 or more separate polypeptide chains combine to form 3D structure.
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NH2
Lysine
Histidin
Valine
Arginine
Alanine
COOH
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The numbers of amino acids vary
(e.g. insulin 51, lysozyme 129, haemoglobin 574, gamma globulin 1250)
Polar amino acids (hydrophillic) tend to be placed on the outside of the protein.
Non-polar (hydrophobic) amino acids tend to be placed on the inside of the protein
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The number of possible sequences is infinite .
An average protein has 300 amino acids.
At each position there could be one of 20 different amino acids = 10390 possible combinations
© 2007 Paul Billiet ODWS
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Polypeptide chains tend to twist or coil upon themselves.
Held together by H bonds. Each amino acid is spatially related to its
neighbour in the same way, is the Secondary Structure of Protein.
It may take any form either α-Helix or β pleated sheet
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The folding of the polypeptide chain occurs using weak hydrogen bonds
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Properties of alpha helix
• It is clockwise , spiral • First -NH and last C=O groups at the ends of helices do not participate in H-
bond• Ends of helices are polar, and almost always at surfaces of proteins• Always right- handed because proteins have L-amino acids.• More stable form.• Easily stretchable.
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This produces the beta pleating The length of the helix or pleat is determined by the number of amino
acids .
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The peptide strands may run in the same direction (Parallel strands)or may be
( anti-parallel strands).They are in elastic because the H bonds are at right angles to the direction of stretching.
Collagen is an example.
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Supersecondary structure (motifs): small, discrete, commonly observed aggregates of secondary structures
sheet
helix-loop-helix
Domains: independent units of structure barrel four-helix bundle
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The folding of the polypeptide and refolded on itself, to give rise to a definite three dimensional confirmation which makes it globular and rigid structure.
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This folding is held together by strong covalent bonds (e.g. cysteine-cysteine disulphide bridge)
H bondingAttraction between COOH group and NH group
Ester linkage between COOH group and a OH group
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Cross linkages can be between 2 parts of a protein or between 2 subunits
Disulfide bonds (S-S) form between adjacent -SH groups on the amino acid cysteine
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The binding site forms when amino acids from within the protein come together in the folding
The remaining sequences may play a role in regulating the protein’s activity
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The quaternary protein structure involves the clustering of several individual peptide or protein chains into a final specific shape. Bonding interactions including hydrogen bonding, salt bridges, and disulfide bonds hold the various chains into a particular geometry.
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• Refers to the organization of subunits in a protein with multiple subunits, may be identical or different.Subunits have a defined arrangement
held together by weak, noncovalent interactions (hydrophobic, H bonds,ionic bonds) .There are two major categories of proteins with quaternary structure - fibrous and globular.
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Fibrous proteins such as the keratins in wool and hair.
Examples of Globular proteins include insulin and hemoglobin.
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Stability: reduction of surface to volume ratio
Bringing catalytic sites together
Structural and functional advantages of quaternary
structure
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Protein structure dictates function. Sometimes a mutation in DNA results in an
amino acid substitution that alters a protein’s structure and compromises its function◦Example: Hemoglobin-S leading to sickle-cell anemia
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VALINE HISTIDINE LEUCINE GLUTAMATEVALINETHREONINE PROLINE
sickle cell
normal cell
One amino acid substitution results in theabnormal beta chain in HbS molecules. Insteadof glutamate, valine was added at the sixthposition of the polypeptide chain.
Normally rounded red blood cells are converted into sickle shapes.
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Primary
Secondary
Tertiary
Quaternary
Assembly
Folding
Packing
Interaction
S T
R U
C T
U R
E P R O C E S S
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Primary structure (Amino acid sequence)↓
Secondary structure ( α-helix, β-sheet )↓
Tertiary structure ( Three-dimensional structure formed by assembly of
secondary structures )↓
Quaternary structure ( Structure formed by many polypeptide chains )
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If a protein unfolds and loses its three-dimensional shape (denatures), it also loses its function
Caused by shifts in pH or temperature, or exposure to detergent or salts ◦ Disrupts hydrogen bonds and other molecular
interactions responsible for protein’s shape
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Denaturation of protein occurs when an egg is cooked
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