The introduction of strain and its effects on the structure and stability of T4 lysozyme
- 7 January 2000
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 295 (1) , 127-145
- https://doi.org/10.1006/jmbi.1999.3300
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Thermodynamic and Structural Compensation in “Size-switch” Core Repacking Variants of Bacteriophage T4 LysozymeJournal of Molecular Biology, 1996
- Determination of α-Helix Propensity within the Context of a Folded ProteinJournal of Molecular Biology, 1994
- The Role of Backbone Flexibility in the Accommodation of Variants That Repack the Core of T4 LysozymeScience, 1993
- Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala .fwdarw. Ser and Val .fwdarw. Thr substitutions in T4 lysozymeBiochemistry, 1993
- Hydrophobic core repacking and aromatic–aromatic interaction in the thermostable mutant of T4 lysozyme ser 117 → pheProtein Science, 1993
- Side-chain entropy opposes alpha-helix formation but rationalizes experimentally determined helix-forming propensities.Proceedings of the National Academy of Sciences, 1992
- Structural and thermodynamic analysis of the packing of two α-helices in bacteriophage T4 lysozymeJournal of Molecular Biology, 1991
- A mutant T4 lysozyme (Val 131 → Ala) designed to increase thermostability by the reduction of strain within an α‐helixProteins-Structure Function and Bioinformatics, 1990
- Thermal denaturation of bacteriophage T4 lysozyme at neutral pHBiopolymers, 1987
- [27] Structure and thermal stability of phage T4 lysozymePublished by Elsevier ,1987