Direct access to the cooperative substructure of proteins and the protein ensemble via cold denaturation
- 29 February 2004
- journal article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 11 (4) , 352-357
- https://doi.org/10.1038/nsmb739
Abstract
The modern view of protein thermodynamics predicts that proteins undergo cold-induced unfolding. Unfortunately, the properties of proteins and water conspire to prevent the detailed observation of this fundamental process. Here we use protein encapsulation to allow cold denaturation of the protein ubiquitin to be monitored by high-resolution NMR at temperatures approaching -35 degrees C. The cold-induced unfolding of ubiquitin is found to be highly noncooperative, in distinct contrast to the thermal melting of this and other proteins. These results demonstrate the potential of cold denaturation as a means to dissect the cooperative substructures of proteins and to provide a rigorous framework for testing statistical thermodynamic treatments of protein stability, dynamics and function.Keywords
This publication has 21 references indexed in Scilit:
- Validation of Protein Structure from Preparations of Encapsulated Proteins Dissolved in Low Viscosity FluidsJournal of the American Chemical Society, 2001
- Toward Structural Biology in Supercooled WaterJournal of the American Chemical Society, 2000
- Cold denaturation of ubiquitinBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1999
- High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluidsProceedings of the National Academy of Sciences, 1998
- Local Stability and Dynamics of Apocytochrome b562 Examined by the Dependence of Hydrogen Exchange on Hydrostatic Pressure,Biochemistry, 1998
- Structure of the Pressure-Assisted Cold Denatured State of UbiquitinBiochemical and Biophysical Research Communications, 1997
- Protein Folding Intermediates: Native-State Hydrogen ExchangeScience, 1995
- Thermodynamics of ubiquitin unfoldingProteins-Structure Function and Bioinformatics, 1994
- Cold Denaturation of ProteinCritical Reviews in Biochemistry and Molecular Biology, 1990
- The cold‐induced denaturation of lactate dehydrogenase at sub‐zero temperatures in the absence of perturbantsFEBS Letters, 1989