Lecture12

Lecture12 - Lecture12 10/19/11 Background Reading: Berg, et...

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Unformatted text preview: Lecture12 10/19/11 Background Reading: Berg, et al.: pages 52 -57 pages 222-224 Garrett and Grisham: page 1028 pages 56 64 Segel: pages 145 - 146 Outline: Post-translational modifications of proteins Motifs/consensus sequences Proteolytic modifications Energetics Factors determining the value of G Standard state Post-translational modifications of proteins After synthesis, proteins can undergo a series of modifications, some of which occur before folding and others after folding. Example: Binding of heme to myoglobin and hemoglobin. Example: Hydroxylation of some proline residues in collagen. Motifs/Consensus sequences Many of the covalent modifications of proteins that occur are dependent upon the ability of the modifying enzyme(s) to recognize particular consensus sequences (motifs) within the protein. Examples: Secretory proteins can be glycosylated on asparagine residues when they enter the secretory system of the cell if they contain a NXS/T motif within their sequence. The consensus sequence recognized by protein kinase A, an enzyme that phosphorylates serine or threonine residues is R R X S Z or R R X T Z, where X is a small amino acid and Z is a large hydrophobic residue. By searching for such motifs in amino acid sequences predicted by the DNA sequence encoding the protein biochemists can make predictions as to whether the protein may have a particular modification or function before it is biochemically detected....
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This note was uploaded on 01/15/2012 for the course BIS 102 taught by Professor Hilt during the Fall '08 term at UC Davis.

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Lecture12 - Lecture12 10/19/11 Background Reading: Berg, et...

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