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Thermodynamics of the binding of biotin and some analogues by avidin
Open accessAbstract
1. The reaction between avidin and biotin was found to be exothermic, DeltaH being -20.3kcal./mole of biotin bound. The corresponding value of DeltaH for streptavidin was -23kcal./mole. 2. The heat evolved was independent of the pH (between 5 and 9), of the buffer (borate or ammonia) and of the fractional saturation of the avidin with biotin. 3. The entropy change for the reaction was zero, and it is suggested that the entropy increase to be expected from hydrophobic interactions was counterbalanced by a decrease in entropy accompanying the formation of buried hydrogen bonds. 4. Modification of the potential hydrogen-bonding sites of the imidazolidone ring led to a decreased heat output and a positive entropy of reaction.
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Cited by
Hou, T., Wang, J., Li, Y., & Wang, W. (2011) · Journal of Chemical Information and Modeling · doi:10.1021/ci100275a · Cited by 2,773
Spiller, K. L., Nassiri, S., Witherel, C. E., Anfang, R. R., Ng, J., Nakazawa, K. R., Yu, T., & Vunjak-Novakovic, G. (2015) · Biomaterials · doi:10.1016/j.biomaterials.2014.10.017 · Cited by 773
Metadata
- Authors
- Green, N.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1966-12-01
- Volume
- 101
- Issue
- 3
- Pages
- 774-780
- ISSN
- 0006-2936 (ISSN-L)
- OpenAlex
- W1892938473
- Cited by
- 202
- References
- 0
- FWCI
- 1.18
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Green, N. (1966). Thermodynamics of the binding of biotin and some analogues by avidin. Biochemical Journal. https://doi.org/10.1042/bj1010774
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
