Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 531, Issue 1-2, Pages 110-115Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2012.11.016
Keywords
Energy landscape; Kinetic intermediates; Equilibrium intermediates; High pressure NMR; Partial molar volume; Activation volume
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Funding
- Academic Frontier Program from the Ministry of Education, Culture, Sports, Science and Technology of Japan [07F010]
- Grants-in-Aid for Scientific Research [24570180] Funding Source: KAKEN
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The unique role of pressure in protein folding studies is emphasized. Variable-pressure NMR experiments carried out under equilibrium conditions give unique opportunities to explore the energy landscape for protein folding. Intermediate conformers that may appear transiently in the kinetic folding experiments may be stably trapped under pressure, allowing examination of their conformations in site-specific detail with modern NMR spectroscopy. The intimate relationship between the kinetic folding experiment and the equilibrium pressure experiment is described with examples from ubiquitin and hen lysozyme. (C) 2012 Elsevier Inc. All rights reserved.
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