Reversible peptide folding in solution by molecular dynamics simulation.

Abstract:

:Long-standing questions on how peptides fold are addressed by the simulation at different temperatures of the reversible folding of a peptide in solution in atomic detail. Molecular dynamics simulations correctly predict the structure that is thermodynamically stable at 298 K, irrespective of the initial peptide conformation. The rate of folding and the free energy of folding at different temperatures are estimated. Although the conformational space potentially accessible to the peptide is extremely large, very few conformers (10(1) to 10(2)) are significantly populated at 20 K above the melting temperature. This implies that the search problem in peptide (or even protein) folding is surmountable using dynamics simulations.

journal_name

J Mol Biol

authors

Daura X,Jaun B,Seebach D,van Gunsteren WF,Mark AE

doi

10.1006/jmbi.1998.1885

subject

Has Abstract

pub_date

1998-07-31 00:00:00

pages

925-32

issue

5

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(98)91885-X

journal_volume

280

pub_type

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