Effects of Structural Modification on the Thermostability of F1 Protease from Bacillus Stearothermophilus F1
A thermophilic Bacillus stearothermophilus F1 was found to produce an extremely thermostable serine protease. The F1 protease sequence was modeled onto the crystal structure of thermitase with 61% sequence identity. The F1 protease contains a catalytic triad comprising of Asp39, His72 and Ser226. T...
Saved in:
| Main Author: | |
|---|---|
| Format: | Thesis |
| Language: | English |
| Published: |
2007
|
| Online Access: | http://ethesis.upm.edu.my/id/eprint/1081/1/FBSB_2007_23.pdf |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|