Advances in molecular simulations of protein mechanical properties and function.

Clicks: 296
ID: 83104
2020
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Ranked #12 of 30 articles by views in current opinion in structural biology

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Abstract
Single-molecule force spectroscopy and classical molecular dynamics are natural allies. Recent advances in both experiments and simulations have increasingly facilitated a direct comparison of SMFS and MD data, most importantly by closing the gap between time scales, which has been traditionally at least 5 orders of magnitudes wide. In this review, we will explore these advances chiefly on the computational side. We focus on protein dynamics under force and highlight recent studies that showcase how lower loading rates and more statistics help to better interpret previous experiments and to also motivate new ones. At the same time, steadily increasing system sizes are used to mimic more closely the mechanical environment in the biological context. We showcase some of these advances on atomistic and coarse-grained scale, from asymmetric membrane tension to larger (multidomain/multimeric) protein assemblies under force.
Reference Key
franz2020advancescurrent Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Franz, Florian;Daday, Csaba;Gräter, Frauke;
Journal current opinion in structural biology
Year 2020
DOI
S0959-440X(19)30154-X
URL
Keywords
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