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J Mol Biol. 2000 Apr 28;298(2):303-12.

Evolutionary conservation in protein folding kinetics.

Author information

1
Department of Biochemistry, University of Washington, Seattle, WA 98195, USA. kwplaxco@u.washington.edu

Abstract

The sequence and structural conservation of folding transition states have been predicted on theoretical grounds. Using homologous sequence alignments of proteins previously characterized via coupled mutagenesis/kinetics studies, we tested these predictions experimentally. Only one of the six appropriately characterized proteins exhibits a statistically significant correlation between residues' roles in transition state structure and their evolutionary conservation. However, a significant correlation is observed between the contributions of individual sequence positions to the transition state structure across a set of homologous proteins. Thus the structure of the folding transition state ensemble appears to be more highly conserved than the specific interactions that stabilize it.

PMID:
10764599
DOI:
10.1006/jmbi.1999.3663
[Indexed for MEDLINE]

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