Boosting protein stability with the computational design of β-sheet surfaces.

ABSTRACT: β-sheets often have one face packed against the core of the protein and the other facing solvent. Mutational studies have indicated that the solvent-facing residues can contribute significantly to protein stability, and that the preferred amino acid at each sequence position is dependent on the precise structure of the protein backbone and the identity of the neighboring amino acids. This suggests that the most advantageous methods for designing β-sheet surfaces will be approaches that take into account the multiple energetic factors at play including side chain rotamer preferences, van der Waals forces, electrostatics, and desolvation effects. Here, we show that the protein design software Rosetta, which models these energetic factors, can be used to dramatically increase protein stabilit

SUBMITTER: Kim DN 

PROVIDER: S-EPMC4815415 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature