Title : Role of a subdomain in the folding of bovine pancreatic trypsin inhibitor.

Pub. Date : 1990 Apr 12

PMID : 1691452






3 Functional Relationships(s)
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1 The disulphide-bonded intermediates that accumulate in the oxidative folding of bovine pancreatic trypsin inhibitor (BPTI) were characterized some time ago. disulphide spleen trypsin inhibitor I Bos taurus
2 The disulphide-bonded intermediates that accumulate in the oxidative folding of bovine pancreatic trypsin inhibitor (BPTI) were characterized some time ago. disulphide spleen trypsin inhibitor I Bos taurus
3 We have tested the hypothesis that the precursor to N* is the one-disulphide intermediate [5-55], which contains the most stable disulphide in BPTI, and present evidence here that this is the case. disulphide spleen trypsin inhibitor I Bos taurus