A funneled energy landscape for cytochrome c directly predicts the sequential folding route inferred from hydrogen exchange experiments.

Abstract:

:Proteins fold through a variety of mechanisms. For a given protein, folding routes largely depend on the protein's stability and its native-state geometry, because the landscape is funneled. These ideas are corroborated for cytochrome c by using a coarse-grained topology-based model with a perfect funnel landscape that includes explicit modeling of the heme. The results show the importance of the heme as a nucleation site and explain the observed hydrogen exchange patterns of cytochrome c within the context of energy landscape theory.

authors

Weinkam P,Zong C,Wolynes PG

doi

10.1073/pnas.0505274102

keywords:

subject

Has Abstract

pub_date

2005-08-30 00:00:00

pages

12401-6

issue

35

eissn

0027-8424

issn

1091-6490

pii

0505274102

journal_volume

102

pub_type

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