Stabilization of λ repressor against thermal denaturation by site‐directed Gly→Ala changes in α‐helix 3

Michael H. Hecht, Julian M. Sturtevant, Robert T. Sauer

Research output: Contribution to journalArticle

106 Scopus citations

Abstract

Oligonucleotide‐directed mutagenesis has been used to replace α‐helical glycines in the N‐terminal domain of λ repressor with alanines. Since alanine is a significantly better helix‐forming residue than glycine, these changes were predicted to have a stabilizing effect. We show that the Gly46→Ala substitution, the Gly48→Ala substitution, and the double substitution increase the melting temperature of the N‐terminal domain by 3–6°.

Original languageEnglish (US)
Pages (from-to)43-46
Number of pages4
JournalProteins: Structure, Function, and Bioinformatics
Volume1
Issue number1
DOIs
StatePublished - Jan 1 1986
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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