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Article

Stabilization of the neutral protease of Bacillus stearothermophilus by removal of a buried water molecule.

Protein engineering - 1 Dec 1991

Vriend G, Berendsen H J, van der Zee J R, van den Burg B, Venema G, Eijsink V G

Abstract excerpt

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...

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Identifiers

PMID: 1817257
DOI: 10.1093/protein/4.8.941

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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