Computational and single-molecule force studies of a macro domain protein reveal a key molecular determinant for mechanical stability.

ABSTRACT: Resolving molecular determinants of mechanical stability of proteins is crucial in the rational design of advanced biomaterials for use in biomedical and nanotechnological applications. Here we present an interdisciplinary study combining bioinformatics screening, steered molecular dynamics simulations, protein engineering, and single-molecule force spectroscopy that explores the mechanical properties of a macro domain protein with mixed alpha + beta topology. The unique architecture is defined by a single seven-stranded beta-sheet in the core of the protein flanked by five alpha-helices. Unlike mechanically stable proteins studied thus far, the macro domain provides the distinct advantage of having the key load-bearing hydrogen bonds (H bonds) buried in the hydrophobic core protected from

SUBMITTER: Guzman DL 

PROVIDER: S-EPMC2836608 | biostudies-literature | 2010 Feb

REPOSITORIES: biostudies-literature