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. Th...
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| Hlavní autor: | |
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| Médium: | Diplomová práce |
| Jazyk: | English English |
| Vydáno: |
2008
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| Témata: | |
| On-line přístup: | http://psasir.upm.edu.my/id/eprint/4926/1/FBSB_2008_1.pdf |
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