Stabilization provided by neighboring strands is critical for the mechanical stability of proteins.

ABSTRACT: Single-molecule force spectroscopy studies and steered molecular dynamics simulations have revealed that protein topology and pulling geometry play important roles in determining the mechanical stability of proteins. Most studies have focused on local interactions that are associated with the force-bearing beta-strands. Interactions mediated by neighboring strands are often overlooked. Here we use Top7 and barstar as model systems to illustrate the critical importance of the stabilization effect provided by neighboring beta-strands on the mechanical stability. Using single-molecule atomic force microscopy, we showed that Top7 and barstar, which have similar topology in their force-bearing region, exhibit vastly different mechanical-stability characteristics. Top7 is mechanically stable and

SUBMITTER: Sharma D 

PROVIDER: S-EPMC2553132 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature