How native-state topology affects the folding of dihydrofolate reductase and interleukin-1beta.

Abstract:

:The overall structure of the transition-state and intermediate ensembles observed experimentally for dihydrofolate reductase and interleukin-1beta can be obtained by using simplified models that have almost no energetic frustration. The predictive power of these models suggests that, even for these very large proteins with completely different folding mechanisms and functions, real protein sequences are sufficiently well designed, and much of the structural heterogeneity observed in the intermediates and the transition-state ensembles is determined by topological effects.

authors

Clementi C,Jennings PA,Onuchic JN

doi

10.1073/pnas.100547897

keywords:

subject

Has Abstract

pub_date

2000-05-23 00:00:00

pages

5871-6

issue

11

eissn

0027-8424

issn

1091-6490

pii

100547897

journal_volume

97

pub_type

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