Abstract
Recent developments in both NMR and X-ray crystallography allow the analysis of commercial enzymes in unprecedented detail. The novel methods provide detailed insights into protein dynamics, establish the existence of special catalytic hydrogen bonds and define the ionization states at the enzyme active site. A more detailed understanding of how the changes in structure are related to altered function should facilitate the design of future commercial enzymes with improved performance for different environmental conditions.
| Original language | English |
|---|---|
| Pages (from-to) | 391-397 |
| Number of pages | 7 |
| Journal | Current Opinion in Biotechnology |
| Volume | 10 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 1 Aug 1999 |
Keywords
- enzyme
- biotechnology
- enzyme active site
- enzyme activity
- enzyme structure
- hydrogen bond
- industry
- molecular dynamics
- nuclear magnetic resonance
- priority journal
- review
- structure activity relation
- X ray crystallography