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© Research
Publication : BMC structural biology

The redundancy of NMR restraints can be used to accelerate the unfolding behavior of an SH3 domain during molecular dynamics simulations

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in BMC structural biology - 24 Nov 2011

Duclert-Savatier N, Martínez L, Nilges M, Malliavin TE

Link to Pubmed [PMID] – 22115427

BMC Struct. Biol. 2011;11:46

The simulation of protein unfolding usually requires recording long molecular dynamics trajectories. The present work aims to figure out whether NMR restraints data can be used to probe protein conformations in order to accelerate the unfolding simulation. The SH3 domain of nephrocystine (nph SH3) was shown by NMR to be destabilized by point mutations, and was thus chosen to illustrate the proposed method.