Potential use of additivity of mutational effects in simplifying protein engineering.
Open Access
- 1 October 1996
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 93 (20) , 10753-10757
- https://doi.org/10.1073/pnas.93.20.10753
Abstract
The problem of rationally engineering protein molecules can be simplified where effects of mutations on protein function are additive. Crystal structures of single and double mutants in the hydrophobic core of gene V protein indicate that structural and functional effects of core mutations are additive when the regions structurally influenced by the mutations do not substantially overlap. These regions of influence can provide a simple basis for identifying sets of mutations that will show additive effects.Keywords
This publication has 26 references indexed in Scilit:
- Tertiary templates for proteins: Use of packing criteria in the enumeration of allowed sequences for different structural classesPublished by Elsevier ,2005
- Two mutations in recombinant Hb β F41(C7)Y, K82 (EF6)D show additive effects in decreasing oxygen affinityxsProtein Science, 1996
- Alanine Scanning Mutagenesis of the α-Helix 115-123 of Phage T4 Lysozyme: Effects on Structure, Stability and the Binding of SolventJournal of Molecular Biology, 1995
- Energetics of protein-protein interactions: Analysis ofthe Barnase-Barstar interface by single mutations and double mutant cyclesJournal of Molecular Biology, 1995
- Structure of the gene V protein of bacteriophage f1 determined by multiwavelength x-ray diffraction on the selenomethionyl protein.Proceedings of the National Academy of Sciences, 1994
- In Vivo Characterization of Mutants of the Bacteriophage f1 Gene V Protein Isolated by Saturation MutagenesisJournal of Molecular Biology, 1994
- Patterns of nonadditivity between pairs of stability mutations in staphylococcal nucleaseBiochemistry, 1993
- Isolation and in vitro characterization of temperature-sensitive mutants of the bacteriophage f1 gene V proteinJournal of Molecular Biology, 1991
- Replacements of Pro 86 in Phage T4 Lysozyme Extend an α-Helix But Do Not Alter Protein StabilityScience, 1988
- Interactive computer graphics: FRODOPublished by Elsevier ,1985