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Dependence of formation of small disulfide loops in two-cysteine peptides on the number and types of intervening amino acids
1989
Journal of Biological Chemistry
Microscopic disulfide-exchange rate constants have been measured for the formation and opening of small disulfide loops in reactions between glutathione and peptides containing 2 cysteines. Twelve cysteine-Xm-cysteine peptides have been studied, where X is an amino acid and m is the number of amino acids between the cysteines. Homopolymers of alanine for m equaling 0-5 are evaluated, as well as X1 and X2 series employing glycine, valine, or proline. Equilibrium constants Kc for loop closing are
pmid:2808384
fatcat:rpn3lqkrwjfq3cf2o5q6nwck4a