Increasing thermal stability of subtilisin from mutations suggested by strongly interacting side-chain clusters.

Abstract excerpt

In this paper we present for seven subtilisin structures a systematic comparison of densely packed side-group clusters (defined as an ensemble of side chains with extensive internal atomic contacts as compared with those made with the surrounding protein environment and measured relative to the maximum possible for each residue type). Spatially consistent clusters are observed at structurally equivalent positions...

Topics

• Amino Acid Sequence
• Crystallography, X-Ray
• Enzyme Stability
• Models, Molecular
• Molecular Sequence Data
• Mutagenesis, Site-Directed
• Mutation
• Point Mutation
• Protein Engineering
• Protein Structure, Tertiary
• Sequence Alignment