The Relationship Between Conservation, Thermodynamic Stability, and Function in the SH3 Domain Hydrophobic Core
- 1 October 2003
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 333 (3) , 641-655
- https://doi.org/10.1016/j.jmb.2003.08.035
Abstract
No abstract availableKeywords
This publication has 47 references indexed in Scilit:
- Core-directed protein designCurrent Opinion in Structural Biology, 2001
- Native protein sequences are close to optimal for their structuresProceedings of the National Academy of Sciences, 2000
- Core-Directed Protein Design. II. Rescue of a Multiply Mutated and Destabilized Variant of UbiquitinBiochemistry, 1999
- Hydrophobic core packing and protein designCurrent Opinion in Chemical Biology, 1998
- Probing the role of packing specificity in protein designProceedings of the National Academy of Sciences, 1997
- A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme.Proceedings of the National Academy of Sciences, 1996
- Active barnase variants with completely random hydrophobic cores.Proceedings of the National Academy of Sciences, 1996
- The Role of Backbone Flexibility in the Accommodation of Variants That Repack the Core of T4 LysozymeScience, 1993
- Dominant forces in protein foldingBiochemistry, 1990
- Alternative packing arrangements in the hydrophobic core of λrepresserNature, 1989