Fast in silico protein folding by introduction of alternating hydrogen bond potentials.

Abstract:

:We accelerate protein folding in all-atom molecular dynamics simulations by introducing alternating hydrogen bond potentials as a supplement to the force field. The alternating hydrogen bond potentials result in accelerated hydrogen bond reordering, which leads to rapid formation of secondary structure elements. The method does not require knowledge of the native state but generates the potentials based on the development of the tertiary structure in the simulation. In protein folding, the formation of secondary structure elements, especially alpha-helix and beta-sheet, is very important, and we show that our method can fold both efficiently and with great speed.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Wolf MG,de Leeuw SW

doi

10.1529/biophysj.107.122192

subject

Has Abstract

pub_date

2008-05-15 00:00:00

pages

3742-7

issue

10

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(08)70377-1

journal_volume

94

pub_type

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