Reliable protein folding on complex energy landscapes: the free energy reaction path.

Abstract:

:A theoretical framework is developed to study the dynamics of protein folding. The key insight is that the search for the native protein conformation is influenced by the rate r at which external parameters, such as temperature, chemical denaturant, or pH, are adjusted to induce folding. A theory based on this insight predicts that 1), proteins with complex energy landscapes can fold reliably to their native state; 2), reliable folding can occur as an equilibrium or out-of-equilibrium process; and 3), reliable folding only occurs when the rate r is below a limiting value, which can be calculated from measurements of the free energy. We test these predictions against numerical simulations of model proteins with a single energy scale.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Lois G,Blawzdziewicz J,O'Hern CS

doi

10.1529/biophysj.108.133132

subject

Has Abstract

pub_date

2008-09-15 00:00:00

pages

2692-701

issue

6

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(08)78414-5

journal_volume

95

pub_type

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