1yzc

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Revision as of 02:32, 25 November 2007

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The solution structure of a redesigned apocytochrome B562 (Rd-apocyt b562) with the N- and a part of the C-terminal helices unfolded

Overview

Using native-state hydrogen-exchange-directed protein engineering and, multidimensional NMR, we determined the high-resolution structure (rms, deviation, 1.1 angstroms) for an intermediate of the four-helix bundle, protein: Rd-apocytochrome b562. The intermediate has the N-terminal helix, and a part of the C-terminal helix unfolded. In earlier studies, we also, solved the structures of two other folding intermediates for the same, protein: one with the N-terminal helix alone unfolded and the other with a, reorganized hydrophobic core. Together, these structures provide a, description of a protein folding pathway with multiple intermediates at, atomic resolution. The two general features for the intermediates are (i), native-like backbone topology and (ii) nonnative side-chain interactions., These results have implications for important issues in protein folding, studies, including large-scale conformation search, -value analysis, and, computer simulations.

About this Structure

1YZC is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

A protein folding pathway with multiple folding intermediates at atomic resolution., Feng H, Zhou Z, Bai Y, Proc Natl Acad Sci U S A. 2005 Apr 5;102(14):5026-31. Epub 2005 Mar 25. PMID:15793003

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