Three-body interactions improve the prediction of rate and mechanism in protein folding models.

Abstract:

:Here we study the effects of many-body interactions on rate and mechanism in protein folding by using the results of molecular dynamics simulations on numerous coarse-grained Calpha-model single-domain proteins. After adding three-body interactions explicitly as a perturbation to a Gō-like Hamiltonian with native pairwise interactions only, we have found (i) a significantly increased correlation with experimental phi values and folding rates, (ii) a stronger correlation of folding rate with contact order, matching the experimental range in rates when the fraction of three-body energy in the native state is approximately 20%, and (iii) a considerably larger amount of three-body energy present in chymotripsin inhibitor than in the other proteins studied.

authors

Ejtehadi MR,Avall SP,Plotkin SS

doi

10.1073/pnas.0403486101

keywords:

subject

Has Abstract

pub_date

2004-10-19 00:00:00

pages

15088-93

issue

42

eissn

0027-8424

issn

1091-6490

pii

0403486101

journal_volume

101

pub_type

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