Abstract
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 thermostability of the enzyme was increased by 0.3 and 1.0-degrees-C, respectively. The Asp249 and Asp290 mutants exhibited a stabilization of 0.6 and 1.2-degrees-C, respectively. The results show the feasibility of stabilizing enzymes by introducing favourable residues at the end of alpha-helices.
Original language | English |
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Pages (from-to) | 165-170 |
Number of pages | 6 |
Journal | Protein Engineering |
Volume | 5 |
Issue number | 2 |
DOIs | |
Publication status | Published - Mar-1992 |
Keywords
- ALPHA-HELIX
- BACILLUS
- HELIX DIPOLE
- NEUTRAL PROTEASE
- THERMOSTABILITY
- BACILLUS-SUBTILIS
- DIPOLE MODEL
- PROTEINS
- THERMOLYSIN
- STABILITY
- STABILIZATION
- RESOLUTION
- EXPRESSION
- MUTATIONS
- CLONING