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Increasing the thermostability of the neutral proteinase of Bacillus stearothermophilus by improvement of internal hydrogen-bonding.
In an attempt to increase the thermostability of the neutral proteinase of Bacillus stearothermophilus the buried Ala-170 was replaced by serine. Molecular-dynamics simulations showed that Ser-170 stabilizes the enzyme by formation of an internal hydrogen bond. In addition, the hydroxy group of Ser-...
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| Auteurs principaux: | , , , , |
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| Format: | Artigo |
| Langue: | Inglês |
| Publié: |
1992
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| Sujets: | |
| Accès en ligne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1132834/ https://ncbi.nlm.nih.gov/pubmed/1637352 |
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