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Chapter !10 - Proteomics Code : KSI0019

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<p style="text-align: center;"><span style="font-size:36px"><strong>&lt;Index of Chapter 10&gt;</strong></span></p>
<p>&nbsp;</p>
<p><span style="color:#0000CD"><strong>Introduction</strong></span></p>
 
<p>- The proteome is the complete set of proteins associated with a sample of living matter. Proteomics deals with the proteins that form the structures of living things, are active in living things, or are produced by living things. or are produced by living things. This includeds their nature, distrivution , activities , interactions , and evloution. Many fields contribute to proteomics.</p>
 
<p>&nbsp;</p>
<p><span style="color:#0000CD"><strong>Protein nature and types</strong></span></p>
 
<p>Proteins are where the action is</p>
 
<p>1. &nbsp;Proteins have a great variety of functions .</p>
 
<p>2. The amino acid sequences of proteins dictate their 3D structures and their folding pathways. (Folding pathway)&nbsp;</p>
 
<p>3. Advances in protein science have spawned the biotechnology industry.&nbsp;</p>
 
<p>&nbsp;</p>
<p><span style="color:#0000CD"><strong>Protein structure</strong></span></p>
 
<p>&nbsp;Backbone or mainchain / sidechain /</p>
 
<p>&gt; Hydrogen bonding &nbsp;/ Hydrophobic interactions/ Disulphide bridges &nbsp;~&nbsp;</p>
 
<p>&nbsp;</p>
 
<p>Different types of residues make different types of interactions , including hydrogen bonds, hydrophobic interactions, and disulphide bridges. Formation of the native structure allows optimal formation of favorable inter-residue and residue- solvent interactions&nbsp;</p>
 
<p>&nbsp;</p>
 
<p>&gt; A protein is a message writeen in a 20 letter alphabets.&nbsp;</p>
 
<p>Helices and sheets</p>
 
<p>&gt; Helices and sheets are recurrent structures, stablized by mainchain hydrogen bonding, that appear in many protein structures.&nbsp;</p>
<p>-The chemical structure of proteins&nbsp;</p>
<p>-Conformation of the polypeptide chain</p>
 
<p>&gt;Diheadral angles.&nbsp;</p>
<p>-Protein folding patterns</p>
 
<p>&gt; Folding patterns.&nbsp;</p>
 
<p>1. Primary structure&nbsp;</p>
 
<p>2. Sencondary structure.</p>
 
<p>3. Tertiary struture</p>
 
<p>4. quanteanry structure .</p>
 
<p>We describe protein folding patterns according to a hierachy&nbsp;of primarym secondary, tertiary and quaternaty sturctures</p>
 
<p>&nbsp;</p>
<p><span style="color:#0000CD"><strong>Post-translational modifications</strong></span></p>
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