Mechanical network in titin immunoglobulin from force distribution analysis.

ABSTRACT: The role of mechanical force in cellular processes is increasingly revealed by single molecule experiments and simulations of force-induced transitions in proteins. How the applied force propagates within proteins determines their mechanical behavior yet remains largely unknown. We present a new method based on molecular dynamics simulations to disclose the distribution of strain in protein structures, here for the newly determined high-resolution crystal structure of I27, a titin immunoglobulin (IG) domain. We obtain a sparse, spatially connected, and highly anisotropic mechanical network. This allows us to detect load-bearing motifs composed of interstrand hydrogen bonds and hydrophobic core interactions, including parts distal to the site to which force was applied. The role of the forc

SUBMITTER: Stacklies W 

PROVIDER: S-EPMC2643529 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature