Article
Increasing the thermostability of a neutral protease by replacing positively charged amino acids in the N-terminal turn of alpha-helices.
Protein engineering - 1 Mar 1992
Eijsink V G, Vriend G, van den Burg B, van der Zee J R, Venema G
Abstract excerpt
The 247-260 and 289-299 alpha-helices of Bacillus subtilis neutral protease have a lysine in their N-terminal turn. These lysines were replaced by Ser or Asp in order to improve electrostatic interactions with the alpha-helix dipole. After replacing Lys by Ser at positions 249 or 290, the thermos...
Topics
- Amino Acid Sequence
- Bacillus subtilis
- Enzyme Stability
- Metalloendopeptidases
- Models, Molecular
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Protein Conformation
- Protein Denaturation