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Article

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

BMC structural biology - 24 Nov 2011

Duclert-Savatier Nathalie, Martínez Leandro, Nilges Michael, Malliavin Thérèse E

Abstract excerpt

BACKGROUND: 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...

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Identifiers

PMID: 22115427
DOI: 10.1186/1472-6807-11-46
PMCID: PMC3274457

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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