Beyond Lumry-Eyring: An unexpected pattern of operational reversibility/irreversibility in protein denaturation

We have found that, contrary to naïve intuition, the degree of operational reversibility in the thermal denaturation of lipase from Thermomyces lanuginosa (an important industrial enzyme) in urea solutions is maximum when the protein is heated several degrees above the end of the temperature‐induced...

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Bibliographic Details
Published in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2008-01, Vol.70 (1), p.19-24
Main Authors: Rodriguez-Larrea, David, Ibarra-Molero, Beatriz, de Maria, Leonardo, Borchert, Torben V., Sanchez-Ruiz, Jose M.
Format: Article
Language:English
Subjects:
aggregation
calorimetry
Calorimetry, Differential Scanning
chemical denaturants
Hot Temperature
irreversibility
kinetic stability
Kinetics
Lipase - chemistry
Protein Denaturation
Proteins - chemistry
reversibility
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Summary:We have found that, contrary to naïve intuition, the degree of operational reversibility in the thermal denaturation of lipase from Thermomyces lanuginosa (an important industrial enzyme) in urea solutions is maximum when the protein is heated several degrees above the end of the temperature‐induced denaturation transition. Upon cooling to room temperature, the protein seems to reach a state with enzymatic activity similar to that of the initial native state, but with higher denaturation temperature and radically different behavior in terms of susceptibility to irreversible denaturation. These results show that patterns of operational reversibility/irreversibility in protein denaturation may be more complex than the often‐taken‐for‐granted, two‐situation classification (reversible vs. irreversible). Furthermore, they are consistent with the possibility of existence of different native or native‐like states separated by high kinetic barriers under native conditions and they suggest experimental procedures to reach and study such “alternative” native states. Proteins 2008. © 2007 Wiley‐Liss, Inc.
ISSN:0887-3585
1097-0134
DOI:10.1002/prot.21572