Evolution of an Antibiotic Resistance Enzyme Constrained by Stability and Activity Trade-offs
Top Cited Papers
- 28 June 2002
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 320 (1), 85-95
- https://doi.org/10.1016/s0022-2836(02)00400-x
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Prediction of functionally important residues based solely on the computed energetics of protein structureJournal of Molecular Biology, 2001
- Extended-spectrum and inhibitor-resistant TEM-type beta-lactamases: mutations, specificity, and three-dimensional structureAntimicrobial Agents and Chemotherapy, 1995
- Remarkable activity enhancement of thermolysin mutantsFEBS Letters, 1995
- A relationship between protein stability and protein function.Proceedings of the National Academy of Sciences of the United States of America, 1995
- Stability and function: two constraints in the evolution of barstar and other proteinsStructure, 1994
- Effect of active site residues in barnase on activity and stabilityJournal of Molecular Biology, 1992
- Analysis of the steric strain in the polypeptide backbone of protein moleculesProteins, 1991
- Enzymes work by solvation substitution rather than by desolvation.Proceedings of the National Academy of Sciences of the United States of America, 1989
- Energetics of enzyme catalysis.Proceedings of the National Academy of Sciences of the United States of America, 1978
- AREAS, VOLUMES, PACKING, AND PROTEIN STRUCTUREAnnual Review of Biophysics and Bioengineering, 1977