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Thermally denatured state determines refolding in lipase: Mutational analysis
Article first published online: 6 APR 2009
DOI: 10.1002/pro.126
Copyright © 2009 The Protein Society
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How to Cite
Ahmad, S. and Rao, N. M. (2009), Thermally denatured state determines refolding in lipase: Mutational analysis. Protein Science, 18: 1183–1196. doi: 10.1002/pro.126
Publication History
- Issue published online: 26 MAY 2009
- Article first published online: 6 APR 2009
- Accepted manuscript online: 6 APR 2009 12:00AM EST
- Manuscript Accepted: 30 MAR 2009
- Manuscript Revised: 23 MAR 2009
- Manuscript Received: 26 FEB 2009
Funded by
- CSIR Junior Fellowship
- NIMTLI grant. Grant Number: #TLP005
Cited in:
- CrossRef
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- 3, , Enhancing the Thermal Robustness of an Enzyme by Directed Evolution: Least Favorable Starting Points and Inferior Mutants Can Map Superior Evolutionary Pathways, ChemBioChem, 2011, 12, 16Direct Link:
- 4, , , , , , , In Vitro Evolved Non-Aggregating and Thermostable Lipase: Structural and Thermodynamic Investigation, Journal of Molecular Biology, 2011, 413, 3, 726
- 5, , , , Stability curves of laboratory evolved thermostable mutants of a Bacillus subtilis lipase, Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics, 2010, 1804, 9, 1850
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