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. 1966 Dec;101(3):774–780. doi: 10.1042/bj1010774

Thermodynamics of the binding of biotin and some analogues by avidin

N M Green 1,*
PMCID: PMC1270186  PMID: 16742458

Abstract

1. The reaction between avidin and biotin was found to be exothermic, ΔH being −20·3kcal./mole of biotin bound. The corresponding value of ΔH 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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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