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Article

Stabilization of Escherichia coli ribonuclease HI by cavity-filling mutations within a hydrophobic core.

Biochemistry - 22 Jun 1993

Ishikawa K, Nakamura H, Morikawa K, Kanaya S

Abstract excerpt

The crystal structure of Escherichia coli ribonuclease HI has a cavity near Val-74 within the protein core. In order to fill the cavity space, we constructed two mutant proteins, V74L and V74I, in which Val-74 was replaced with either Leu or Ile, respectively. The mutant proteins are stabilized, as revealed by a 2.1-3.7 degrees C increase in the Tm values, as compared to the wild-type protein at pH values of 3.0...

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PMID: 8390295

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

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