Effect of single amino acid replacements on the thermal stability of the NH2-terminal domain of phage lambda repressor.
- 1 September 1984
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 81 (18), 5685-5689
- https://doi.org/10.1073/pnas.81.18.5685
Abstract
The thermal stabilities of mutant phage .lambda. repressors that have single amino acid replacements in the NH2-terminal domain were 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. Mutant proteins bearing solvent-exposed substitutions have thermal stabilities identical to wild type; buried substitutions reduce stability. In 1 case, a single amino acid replacemnt increases the thermal stability of the repressor.This publication has 14 references indexed in Scilit:
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