Micro- and macro-stabilities of globular proteins
β Scribed by PRIVALOV, P. L.; TSALKOVA, T. N.
- Book ID
- 109715897
- Publisher
- Nature Publishing Group
- Year
- 1979
- Tongue
- English
- Weight
- 494 KB
- Volume
- 280
- Category
- Article
- ISSN
- 0028-0836
- DOI
- 10.1038/280693a0
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## Abstract An understanding of the forces that contribute to stability is pivotal in solving the proteinβfolding problem. Classical theory suggests that disulfide bonds stabilize proteins by reducing the entropy of the denatured state. More recent theories have attempted to expand this idea, sugge
The interpretation of A C 3 O (the free energy change for the reaction, globular conformation + randomly coiled conformation, in the absence of denaturant), in terms of the free energies of transfer of various parts of the protein molecule from water to denaturant solution, is unsatisfactory because