Lecture Notes 9-29-08 - Protein Phosphorylation Protein...

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Protein Phosphorylation Protein function can be regulated by the covalent addition of a phosphate group to one of its amino acid side chains Each phosphate group carries 2 negative charges, which can attract local positively charged amino acid side chains and cause a conformational change in the protein that alters the binding site An attached phosphate group can form part of a structure that is directly recognized by binding sites of other proteins Protein kinases are enzymes that transfer the terminal phosphate group of an ATP molecule to the hydroxyl group of a serine, threonine, or tyrosine side chain of the protein Protein phosphatases remove phosphate groups from proteins
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Many thousands of proteins in a typical eucaryotic cell are modified by the covalent addition of a phosphate group A phosphate group from ATP is transferred to an amino acid side chain of the target protein by a protein kinase In this example, the phosphate is added to a serine side chain
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This note was uploaded on 02/22/2010 for the course BE 2400 taught by Professor Goldman during the Fall '08 term at Michigan Technological University.

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Lecture Notes 9-29-08 - Protein Phosphorylation Protein...

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