Universality classes in folding times of proteins.

Abstract:

:Molecular dynamics simulations in simplified models allow one to study the scaling properties of folding times for many proteins together under a controlled setting. We consider three variants of the Go models with different contact potentials and demonstrate scaling described by power laws and no correlation with the relative contact order parameter. We demonstrate existence of at least three kinetic universality classes that are correlated with the types of structure: the alpha-, alpha-beta-, and beta- proteins have the scaling exponents of approximately 1.7, 2.5, and 3.2, respectively. The three classes merge into one when the contact range is truncated at a reasonable value. We elucidate the role of the potential associated with the chirality of a protein.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Cieplak M,Hoang TX

doi

10.1016/S0006-3495(03)74867-X

subject

Has Abstract

pub_date

2003-01-01 00:00:00

pages

475-88

issue

1

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(03)74867-X

journal_volume

84

pub_type

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