A simplified model of local structure in aqueous proline amino acid revealed by first-principles molecular dynamics simulations.

Abstract:

:Aqueous proline solutions are deceptively simple as they can take on complex roles such as protein chaperones, cryoprotectants, and hydrotropic agents in biological processes. Here, a molecular level picture of proline/water mixtures is developed. Car-Parrinello ab initio molecular dynamics (CPAIMD) simulations of aqueous proline amino acid at the B-LYP level of theory, performed using IBM's Blue Gene/L supercomputer and massively parallel software, reveal hydrogen-bonding propensities that are at odds with the predictions of the CHARMM22 empirical force field but are in better agreement with results of recent neutron diffraction experiments. In general, the CPAIMD (B-LYP) simulations predict a simplified structural model of proline/water mixtures consisting of fewer distinct local motifs. Comparisons of simulation results to experiment are made by direct evaluation of the neutron static structure factor S(Q) from CPAIMD (B-LYP) trajectories as well as to the results of the empirical potential structure refinement reverse Monte Carlo procedure applied to the neutron data.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Troitzsch RZ,Tulip PR,Crain J,Martyna GJ

doi

10.1529/biophysj.108.134916

subject

Has Abstract

pub_date

2008-12-01 00:00:00

pages

5014-20

issue

11

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(08)78928-8

journal_volume

95

pub_type

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