Stabilization of λ repressor against thermal denaturation by site‐directed Gly→Ala changes in α‐helix 3
- 1 January 1986
- journal article
- research article
- Published by Wiley in Proteins-Structure Function and Bioinformatics
- Vol. 1 (1) , 43-46
- https://doi.org/10.1002/prot.340010108
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°.Keywords
This publication has 16 references indexed in Scilit:
- Effect of side chain-backbone electrostatic interactions on the stability of alpha-helices.Proceedings of the National Academy of Sciences, 1985
- Increasing and decreasing protein stability: Effects of revertant substitutions on the thermal denaturation of phage λ repressorJournal of Cellular Biochemistry, 1985
- The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus)Cell, 1984
- Cloning vectors that yield high levels of single-stranded DNA for rapid DNA sequencingGene, 1984
- Vectors bearing a hybrid trp-lac promoter useful for regulated expression of cloned genes in Escherichia coliGene, 1983
- [32] Oligonucleotide-directed mutagenesis of DNA fragments cloned into M13 vectorsPublished by Elsevier ,1983
- The operator-binding domain of λ repressor: structure and DNA recognitionNature, 1982
- [76] Bacteriophage λ repressor and cro protein: Interactions with operator DNAPublished by Elsevier ,1980
- Conformation of Polypeptides and ProteinsPublished by Elsevier ,1968
- Conformational energy estimates for statistically coiling polypeptide chainsJournal of Molecular Biology, 1967