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Dominant forces in protein folding
Abstract
T e purpose of this review is to assess the nature and mag-nitudes of the dominant forces in protein folding. Since proteins are only marginally stable at room temperature, ’ no type of molecular interaction is unimportant, and even small interactions can contribute significantly (positively or nega-tively) to stability (Alber, 1989a,b; Matthews, 1987a,b). However, the present review aims to identify only the largest forces that lead to the structural features of globular proteins: their extraordinary compactness, their core of nonpolar resi-dues, and their considerable amounts of internal architecture. This review explores contributions to the free energy of folding arising from electrostatics (classical charge repulsions and ion pairing), hydrogen-bonding and van der Waals in-teractions, intrinsic propensities, and hydrophobic interactions. An earlier review by Kauzmann (1959) introduced the im-
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Metadata
- Authors
- Dill, K. A.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1990-08-07
- Volume
- 29
- Issue
- 31
- Pages
- 7133-7155
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2070783701
- Cited by
- 3,800
- References
- 2
- FWCI
- 28.36
- Type
- journal article
- Language
- en
- Open access
- closed
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