Effect of single amino acid replacements on the thermal stability of the NH2-terminal domain of phage λ repressor

M. H. Hecht, J. M. Sturtevant, R. T. Sauer

Research output: Contribution to journalArticle

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Abstract

The thermal stabilities of mutant phage λ repressors that have single amino acid replacements in the NH2-terminal domain have been studied by means of circular dichroism and differential scanning calorimetry. The variations in stability determined by these physical methods correlate with the resistance to proteolysis at various temperatures and can be compared with the temperature-sensitive activity of the mutants in vivo. In general, mutant proteins bearing solvent-exposed substitutions have thermal stabilities identical to wild type, whereas buried substitutions reduce stability. In one case, a single amino acid replacement increases the thermal stability of the repressor.

Original languageEnglish (US)
Pages (from-to)5685-5689
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume81
Issue number18 I
DOIs
StatePublished - Jan 1 1984
Externally publishedYes

All Science Journal Classification (ASJC) codes

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