Article
Stabilization of the neutral protease of Bacillus stearothermophilus by removal of a buried water molecule.
Protein engineering - 1 Dec 1991
Vriend G, Berendsen H J, van der Zee J R, van den Burg B, Venema G, Eijsink V G
Abstract excerpt
Using site-directed mutagenesis, Ala166 in the neutral protease of Bacillus stearothermophilus was changed into Ser. Model building and molecular dynamics simulations of the mutant enzyme indicated that the Ser hydroxyl group fits well in a cavity which contains a water molecule in the wild-type...
Topics
- Alanine
- Bacterial Proteins
- Base Sequence
- Enzyme Stability
- Geobacillus stearothermophilus
- Hydrogen Bonding
- Metalloendopeptidases
- Models, Molecular
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Protein Conformation
- Serine
- Water
