Elasticity, structure, and relaxation of extended proteins under force.

ABSTRACT: Force spectroscopies have emerged as a powerful and unprecedented tool to study and manipulate biomolecules directly at a molecular level. Usually, protein and DNA behavior under force is described within the framework of the worm-like chain (WLC) model for polymer elasticity. Although it has been surprisingly successful for the interpretation of experimental data, especially at high forces, the WLC model lacks structural and dynamical molecular details associated with protein relaxation under force that are key to the understanding of how force affects protein flexibility and reactivity. We use molecular dynamics simulations of ubiquitin to provide a deeper understanding of protein relaxation under force. We find that the WLC model successfully describes the simulations of ubiquitin, espe

SUBMITTER: Stirnemann G 

PROVIDER: S-EPMC3593838 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature