Journal
ANNUAL REVIEW OF PHYSICAL CHEMISTRY, VOL 62
Volume 62, Issue -, Pages 257-277Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-physchem-032210-103531
Keywords
protein folding; urea; guanidinium chloride; hydrophobic effect; FRET; molecular dynamics simulations; single-molecule spectroscopy
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Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM080515] Funding Source: NIH RePORTER
- NIGMS NIH HHS [R01 GM080515, R01GM080515, R01 GM080515-04] Funding Source: Medline
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Protein stability often is studied in vitro through the use of urea and guanidinium chloride, chemical cosolvents that disrupt protein native structure. Much controversy still surrounds the underlying mechanism by which these molecules denature proteins. Here we review current thinking on various aspects of chemical denaturation. We begin by discussing classic models of protein folding and how the effects of denaturants may fit into this picture through their Modulation Of the collapse, or coil-globule transition, which typically. precedes folding. Subsequently, we examine recent molecular dynamics simulations that have shed new light on the possible microscopic origins of the solvation effects brought on by denaturants. It seems likely that both denaturants operate by facilitating solvation of hydrophobic regions of proteins. Finally, we present recent single-molecule fluorescence studies of denatured proteins, the analysis of which corroborates the role of denaturants in shifting the equilibrium of the coil-globule transition.
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