Unique elastic properties of the spectrin tetramer as revealed by multiscale coarse-grained modeling.

Proceedings of the National Academy of Sciences of the United States of America
Dina T Mirijanian, Gregory A Voth

Abstract

The force-extension profile of tetrameric spectrin is determined by using multiscale computer simulation. Fluctuation results of atomistic simulations of double spectrin repeat units (DSRU) are used to systematically build a coarse-grained (CG) model for the tetrameric form of spectrin. It is found that the spectrin tetramer can be modeled as a soft polymer with a unique flat force-extension profile over the range of biologically important lengths. It is also concluded that in the cytoskeletal network of the red blood cell the tetramer is in an "overcompressed" state. These findings are in contrast to the commonly used models of spectrin tetramer elasticity, namely the "entropic spring" polymer models. From these results, it is concluded that stable intact helical linker regions are needed to maintain the soft elasticity of the spectrin tetramer.

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Citations

Dec 29, 2010·Journal of Biomechanical Engineering·Alexandre Lewalle, Kim H Parker
Aug 9, 2008·Science·Michael L Klein, Wataru Shinoda
Oct 26, 2010·The Journal of Chemical Physics·Anatoly M Ruvinsky, Ilya A Vakser
Jun 1, 2010·Computer Methods in Applied Mechanics and Engineering·Dmitry A FedosovGeorge Em Karniadakis
Aug 13, 2014·Scientific Reports·Elena KozlovaArtem Kuzovlev
Sep 23, 2008·Biophysical Journal·Jim Pfaendtner, Gregory A Voth
Jun 13, 2015·PLoS Computational Biology·Jeffrey W BrownC James McKnight
Nov 24, 2018·Protein Science : a Publication of the Protein Society·Dominique Mias-LucquinOlivier Delalande
Feb 6, 2021·Biological Chemistry·Frederik BarbarinoMiriam M Cortese-Krott
May 1, 2020·Journal of Molecular Biology·Jianchao LiMingjie Zhang
Apr 30, 2009·Journal of Cell Science·Julien ColombelliErnst H K Stelzer

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