Thermodynamics of the binding of biotin and some analogues by avidin.

The Biochemical journal ·Vol. 101 ·No. 3 ·1966-12-00 ·Pages 774-80

Green NM

Abstract

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.

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Green N M

Laboratory of Chemistry, National Institute for Arthritis and Metabolic Diseases, National Institutes of Health, Bethesda 14, U.S.A.

References (15)

15 references, click to expand

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Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1010774

Published

1966-12-00

Pages

774-80

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1270186

External Links

PubMed source DOI: 10.1042/bj1010774 PMC Full Text View journal details

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Thermodynamics of the binding of biotin and some analogues by avidin.

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