Functionally acceptable substitutions in two α‐helical regions of λ repressor

John F. Reidharr‐Olson, Robert T. Sauer

Research output: Contribution to journalArticlepeer-review

68 Scopus citations

Abstract

A method of targeted random mutagenesis has been used in investigate the informational content of 25 residue positions in two α‐helical regions of the N‐terminal domain of λ repressor. Examination of the functionally allowed sequences indicates that there is a wide range in tolerance to amino acid substitution at these position. At position that are buried in the structure, there are severe limitations on the number and type of residues allowed. At most surface positions, many different residues and residue types are tolerated. However, at several surface positions there is a string preference for hydrophilic amino acids, and at one surface position proline is absolutely conserved. The results reveal the high level of degeneracy in the information that specifies a particular protein fold.

Original languageEnglish (US)
Pages (from-to)306-316
Number of pages11
JournalProteins: Structure, Function, and Bioinformatics
Volume7
Issue number4
DOIs
StatePublished - 1990

Keywords

  • neutral mutations
  • protein families
  • protein folding
  • protein structure
  • random mutagenesis

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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