Article
Phi-values for BPTI folding intermediates and implications for transition state analysis.
Nature structural biology - 1 Apr 2001
Bulaj G, Goldenberg D P
Abstract excerpt
Amino acid replacements were used to probe the roles of 14 sites in two well-characterized intermediates in the folding pathway of bovine pancreatic trypsin inhibitor (BPTI). One of these intermediates contains one of the three disulfides found in the native protein (30--51). NMR studies have shown that approximately two-thirds of this polypeptide has a native-like conformation. The other intermediate contains...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.