Dynamic stability of salt stable cowpea chlorotic mottle virus capsid protein dimers and pentamers of dimers.

ABSTRACT: Intermediates of the self-assembly process of the salt stable cowpea chlorotic mottle virus (ss-CCMV) capsid can be modelled atomistically on realistic computational timescales either by studying oligomers in equilibrium or by focusing on their dissociation instead of their association. Our previous studies showed that among the three possible dimer interfaces in the icosahedral capsid, two are thermodynamically relevant for capsid formation. The aim of the current study is to evaluate the relative structural stabilities of the three different ss-CCMV dimers and to find and understand the conditions that lead to their dissociation. Long timescale molecular dynamics simulations at 300 K of the various dimers and of the pentamer of dimers underscore the importance of large contact surfaces o

SUBMITTER: Szoverfi J 

PROVIDER: S-EPMC9395436 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature