Unfolding and folding internal friction of β-hairpins is smaller than that of α-helices

The Journal of Physical Chemistry. B
Julius C F SchulzRoland R Netz

Abstract

By the forced unfolding of polyglutamine and polyalanine homopeptides in competing α-helix and β-hairpin secondary structures, we disentangle equilibrium free energetics from nonequilibrium dissipative effects. We find that α-helices are characterized by larger friction or dissipation upon unfolding, regardless of whether they are free energetically preferred over β-hairpins or not. Our analysis, based on MD simulations for atomistic peptide models with explicit water, suggests that this difference is related to the internal friction and mostly caused by the different number of intrapeptide hydrogen bonds in the α-helix and β-hairpin states.

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Citations

Jan 16, 2016·The Journal of Physical Chemistry. B·Guangfeng Zhou, Vincent Alvin Voelz
Mar 8, 2016·The Journal of Physical Chemistry Letters·Wenwei ZhengRobert B Best
Mar 2, 2016·Journal of Chemical Theory and Computation·Hailey R BureauRigoberto Hernandez
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Apr 21, 2017·Journal of Peptide Science : an Official Publication of the European Peptide Society·Bhupesh GoyalSusheel Durani
Feb 23, 2017·Proceedings of the National Academy of Sciences of the United States of America·Andrea SorannoBenjamin Schuler
Mar 11, 2021·The Journal of Physical Chemistry. B·Chenliang XiaWei Wang
Mar 20, 2020·Biophysical Journal·Noah R CohenC R Matthews
Nov 9, 2018·The Journal of Physical Chemistry. B·Fernando Bruno da SilvaVitor B P Leite
Sep 13, 2018·The Journal of Physical Chemistry. B·V M Hridya, Arnab Mukherjee

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