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Numerical Simulation of the Pressure Denaturation of a Helical β ‐Peptide Heptamer Solvated in Methanol
Author(s) -
Gee Peter J.,
van Gunsteren Wilfred F.
Publication year - 2006
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.200690048
Subject(s) - chemistry , peptide , molecular dynamics , denaturation (fissile materials) , methanol , high pressure , crystallography , thermodynamics , computational chemistry , organic chemistry , biochemistry , physics , nuclear chemistry
The effect of elevated pressure on the conformational behavior of a β ‐peptide heptamer ( 1 ) in MeOH solution was considered. The response of the peptide to elevated pressure was probed by means of molecular dynamics (MD) simulations, and described in atomic terms. The most‐striking features of the response are that the region of the ‘unfolded’ state of the peptide accessible at elevated pressure is narrow, and that thermal and pressure denaturation produce similar ‘unfolded’ states in the case of 1 .