找到合适的褶皱。

Finding the right fold.

作者信息

Goldenberg D P

机构信息

Department of Biology, University of Utah, 257 South 1400 East, Salt Lake City, Utah 84112-0840, USA.

出版信息

Nat Struct Biol. 1999 Nov;6(11):987-90. doi: 10.1038/14866.

DOI:10.1038/14866

PMID:10542081

Abstract

Using mutational analysis, three groups have compared the transition states for the folding of two pairs of homologous proteins. The results of these studies suggest that protein folding mechanisms are conserved and are defined primarily by the overall topology of the native structures, as opposed to specific details of the interactions stabilizing these structures.

摘要

通过突变分析，三个研究小组比较了两对同源蛋白质折叠的过渡态。这些研究结果表明，蛋白质折叠机制是保守的，主要由天然结构的整体拓扑结构决定，而非稳定这些结构的相互作用的具体细节。