STABILIZATION OF THE NEUTRAL PROTEASE OF BACILLUS-STEAROTHERMOPHILUS BY REMOVAL OF A BURIED WATER MOLECULE

Ser mutation was expected to exert a stabilizing effect because of the gain in entropy resulting from the release of a water molecular from the folded protein to the solvent. In addition, the hydrogen-bonding network around residue 166 was improved upon the mutation. As a result of this mutation the thermostability of the neutral protease was increased by 1.2 +/- 0.1-degrees-C. -->
Jazyk: English
ISSN: 0269-2139
Přístupová URL adresa: https://explore.openaire.eu/search/publication?articleId=narcis______::d124d87a38a7daef0cae016248fa4a0e
https://research.rug.nl/en/publications/272cb7ad-7481-47d7-92ea-a70ce34edc4b
Rights: RESTRICTED
Přírůstkové číslo: edsair.narcis........d124d87a38a7daef0cae016248fa4a0e
Autor: VRIEND, G, BERENDSEN, HJC, VANDERZEE, [No Value], VANDENBURG, B, VENEMA, G, EIJSINK, VGH
Jazyk: angličtina
Rok vydání: 1991
Předmět:
Zdroj: Protein Engineering, 4(8), 941-945
ISSN: 0269-2139
Popis: Using site-directed mutagenesis, Ala166 in the neutral protease of Bacillus stearothermophilus was changed into Ser. Model building and molecular dynamics simulations of the mutant enzyme indicated that the Ser hydroxyl group fits well in a cavity which contains a water molecule in the wild-type enzyme. The Ala166 --> Ser mutation was expected to exert a stabilizing effect because of the gain in entropy resulting from the release of a water molecular from the folded protein to the solvent. In addition, the hydrogen-bonding network around residue 166 was improved upon the mutation. As a result of this mutation the thermostability of the neutral protease was increased by 1.2 +/- 0.1-degrees-C.
Databáze: OpenAIRE
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