Protein unfolding under force: Crack propagation in a network

Adam M R De Graff, Gareth Shannon, Daniel W. Farrell, Philip M. Williams, Michael Thorpe

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

The mechanical unfolding of a set of 12 proteins with diverse topologies is investigated using an all-atom constraint-based model. Proteins are represented as polypeptides cross-linked by hydrogen bonds, salt bridges, and hydrophobic contacts, each modeled as a harmonic inequality constraint capable of supporting a finite load before breaking. Stereochemically acceptable unfolding pathways are generated by minimally overloading the network in an iterative fashion, analogous to crack propagation in solids. By comparing the pathways to those from molecular dynamics simulations and intermediates identified from experiment, it is demonstrated that the dominant unfolding pathways for 9 of the 12 proteins studied are well described by crack propagation in a network.

Original languageEnglish (US)
Pages (from-to)736-744
Number of pages9
JournalBiophysical journal
Volume101
Issue number3
DOIs
StatePublished - Aug 3 2011

ASJC Scopus subject areas

  • Biophysics

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