Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability
- 8 October 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 292 (5) , 1111-1120
- https://doi.org/10.1006/jmbi.1999.3102
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- [19] Rapid and efficient site-specific mutagenesis without phenotypic selectionPublished by Elsevier ,2004
- Determination of α-Helix Propensity within the Context of a Folded ProteinJournal of Molecular Biology, 1994
- Similar Hydrophobic Replacements of Leu99 and Phe153 within the Core of T4 Lysozyme Have Different Structural and Thermodynamic ConsequencesJournal of Molecular Biology, 1993
- A cavity-containing mutant of T4 lysozyme is stabilized by buried benzeneNature, 1992
- Response of a Protein Structure to Cavity-Creating Mutations and Its Relation to the Hydrophobic EffectScience, 1992
- Improved methods for building protein models in electron density maps and the location of errors in these modelsActa Crystallographica Section A Foundations of Crystallography, 1991
- Temperature-sensitive mutations of bacteriophage T4 lysozyme occur at sites with low mobility and low solvent accessibility in the folded proteinBiochemistry, 1987
- A lysoplate assay for Escherichia coli cell wall-active enzymesAnalytical Biochemistry, 1985
- Computation of molecular volumeJournal of the American Chemical Society, 1985
- [27] Multiwire area X-ray diffractometersPublished by Elsevier ,1985