Title : Development of a novel method to populate native disulfide-bonded intermediates for structural characterization of proteins: implications for the mechanism of oxidative folding of RNase A.

Pub. Date : 2002 May 8

PMID : 11982363






3 Functional Relationships(s)
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1 Development of a novel method to populate native disulfide-bonded intermediates for structural characterization of proteins: implications for the mechanism of oxidative folding of RNase A. Disulfides ribonuclease A family member 1, pancreatic Homo sapiens
2 RNase A, a model protein for oxidative folding studies, has four native disulfide bonds. Disulfides ribonuclease A family member 1, pancreatic Homo sapiens
3 The application of this method enabled us to populate and, in turn, study the key intermediates with two native disulfide bonds on the oxidative folding pathway of RNase A; it also facilitated the isolation of des [58-110] and des [26-84], the other two native-like structured des species whose isolation had thus far not been possible. Disulfides ribonuclease A family member 1, pancreatic Homo sapiens