Enhanced protein thermostability from designed mutations that interact with α-helix dipoles
- 1 December 1988
- journal article
- Published by Springer Nature in Nature
- Vol. 336 (6200), 651-656
- https://doi.org/10.1038/336651a0
Abstract
Two different genetically engineered amino-acid substitutions designed to interact with alpha-helix dipoles in T4 lysozyme are shown to increase the thermal stability of the protein. Crystallographic analyses of the mutant lysozyme structures suggest that the stabilization is due to electrostatic interaction and does not require precise hydrogen bonding between the substituted amino acid and the end of the alpha-helix.Keywords
This publication has 36 references indexed in Scilit:
- Disulfide bonds and thermal stability in T4 lysozyme.Proceedings of the National Academy of Sciences, 1988
- Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding.Proceedings of the National Academy of Sciences, 1987
- Protein engineering of subtilisin BPN': enhanced stabilization through the introduction of two cysteines to form a disulfide bondBiochemistry, 1987
- A new way of enhancing the thermostability of proteasesNature, 1986
- An engineered intersubunit disulfide enhances the stability and DNA binding of the N-terminal domain of .lambda. repressorBiochemistry, 1986
- A structure—function study of dihydrofolate reductase by protein engineeringPhilosophical Transactions of the Royal Society of London. Series A, Mathematical and Physical Sciences, 1986
- Stabilization of λ repressor against thermal denaturation by site‐directed Gly→Ala changes in α‐helix 3Proteins-Structure Function and Bioinformatics, 1986
- The design and production of semisynthetic ribonucleases with increased thermostability by incorporation of S‐peptide analogues with enhanced helical stabilityProteins-Structure Function and Bioinformatics, 1986
- A genetic screen for mutations that increase the thermal stability of phage T4 lysozyme.Proceedings of the National Academy of Sciences, 1985
- Disulfide Bond Engineered into T4 Lysozyme: Stabilization of the Protein Toward Thermal InactivationScience, 1984