lecture 5 - Carb peptidase a does not like lyc or arg at...

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Carb peptidase a does not like lyc or arg at all, has hydrophobic side. Will cleave all acids from the c terminus, except. Proline cannot be cleaved by any of peptidases. Proline on either side of the peptide makes cleavage difficult. Proline has secondary amine structure cyclic. Edman degradation-chemical is exopeptidic cleavage. From amino terminal N. Carboxy peptidase--- recessive, as they start they keep going until they hit what they cant cleave. Edman ---strategy is that u cant just throw and expect it to cleave it sequentially, it will cleave only up to thiazolione, only in presence of water it can rearrange itself. Edman reagent---useful for sequencing from amino terminal all the way down pelipeptide change. Three dimensional structure: when you have in repeating structural motif---secondary structure alpha helix. Tertiary---overall folding. Some regions of repeated, and some as non-helical or non-beta sheet like. There is considerable constrain in which amino arrange. The chain of amino acids is limited in rotation sp2 . coplanar atoms. There is rotation about NC alpha bond, and Calpha O bond. The actual arrangement can be described precisely in dihydral angles which are characteristics to all of the chains. Ramachandran plot: reveals allowed positions. Energy countours, until they overlap. Grey is disallowed
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This note was uploaded on 01/30/2010 for the course BIO 351 taught by Professor Hoffmann,j during the Fall '08 term at SUNY Stony Brook.

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lecture 5 - Carb peptidase a does not like lyc or arg at...

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