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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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Main Authors: Eijsink, V G, Vriend, G, Van der Zee, J R, Van den Burg, B, Venema, G
格式: Artigo
語言:Inglês
出版: 1992
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在線閱讀:https://ncbi.nlm.nih.gov/pmc/articles/PMC1132834/
https://ncbi.nlm.nih.gov/pubmed/1637352
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