Journal article
Interpreting the Effects of Small Uncharged Solutes on Protein-Folding Equilibria
Annual review of biophysics and biomolecular structure, v 30(1), 271
01 Jan 2001
PMID: 11340061
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Proteins are designed to function in environments crowded by cosolutes, but most studies of protein equilibria are conducted in dilute solution. While there is no doubt that crowding changes protein equilibria, interpretations of the changes remain controversial. This review combines experimental observations on the effect of small uncharged cosolutes (mostly sugars) on protein stability with a discussion of the thermodynamics of cosolute-induced nonideality and critical assessments of the most commonly applied interpretations. Despite the controversy surrounding the most appropriate manner for interpreting these effects of thermodynamic nonideality arising from the presence of small cosolutes, experimental advantage may still be taken of the ability of the cosolute effect to promote not only protein stabilization but also protein self-association and complex formation between dissimilar reactants. This phenomenon clearly has potential ramifications in the cell, where the crowded environment could well induce the same effects.
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Details
- Title
- Interpreting the Effects of Small Uncharged Solutes on Protein-Folding Equilibria
- Creators
- Paula R. Davis-Searles - University of North Carolina at Chapel HillAleister J. Saunders - University of North Carolina at Chapel HillDorothy A. Erie - University of North Carolina at Chapel HillDonald J. Winzor - University of North Carolina at Chapel HillGary J. Pielak - University of North Carolina at Chapel Hill
- Publication Details
- Annual review of biophysics and biomolecular structure, v 30(1), 271
- Publisher
- Annual Reviews
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biology
- Web of Science ID
- WOS:000169531600013
- Scopus ID
- 2-s2.0-0034987618
- Other Identifier
- 991021448172404721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics