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Journal article
Polarity of disulfide bonds
Protein science, v 2(7), pp 1183-1184
Jul 1993
PMID: 8358301
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Abstract
Protein stability is defined as the free energy of denatured state minus that of the native state, AGd. Flory (1956) proposed that disulfide bonds increase AGd by decreasing chain entropy in the denatured state. Alternatively, Doig and Williams (1991) suggest that the increase in AGd of proteins by disulfide bonds is primarily enthalpic. Whatever the source of the stabilization, proteins with naturally occurring disulfide bonds are more stable than their noncross-linked equivalents (Pace et al., 1988). Introduction of novel disulfides, however, does not always stabilize proteins (Betz & Pielak [1992] and references therein). [1st paragraph]
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Details
- Title
- Polarity of disulfide bonds
- Creators
- Aleister J. Saunders - University of North Carolina at Chapel HillGregory B. Young - University of North Carolina at Chapel HillGary J. Pielak - University of North Carolina at Chapel Hill
- Publication Details
- Protein science, v 2(7), pp 1183-1184
- Publisher
- Wiley
- Number of pages
- 2
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biology
- Web of Science ID
- WOS:A1993LJ92900013
- Scopus ID
- 2-s2.0-0027276934
- Other Identifier
- 991021448047204721
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- Web of Science research areas
- Biochemistry & Molecular Biology