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The protein folding transition state: what are Phi-values really telling us?

作者信息

Raleigh Daniel P, Plaxco Kevin W

机构信息

Department of Chemistry, Graduate Program in Biochemistry and Structural Biology, State University of New York at Stony Brook, NY 11794-3400, USA.

出版信息

Protein Pept Lett. 2005 Feb;12(2):117-22. doi: 10.2174/0929866053005809.

DOI:10.2174/0929866053005809
PMID:15723637
Abstract

Protein engineering-based studies of the folding transition state have accelerated significantly in the last decade, and more than a half dozen proteins have been subjected to extensive Phi-value analysis. A general picture is emerging from these studies of a transition state in which the large majority of experimentally characterized side chains participate in relatively homogeneous and energetically weak interactions playing only a relatively small role in defining relative folding rates.

摘要

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