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Titolo:
Direct measurement of protein binding energetics by isothermal titration calorimetry
Autore:
Leavitt, S; Freire, E;
Indirizzi:
Johns Hopkins Univ, Dept Biol, Baltimore, MD 21218 USA Johns Hopkins UnivBaltimore MD USA 21218 t Biol, Baltimore, MD 21218 USA Johns Hopkins Univ, Ctr Biocalorimetry, Baltimore, MD 21218 USA Johns Hopkins Univ Baltimore MD USA 21218 imetry, Baltimore, MD 21218 USA
Titolo Testata:
CURRENT OPINION IN STRUCTURAL BIOLOGY
fascicolo: 5, volume: 11, anno: 2001,
pagine: 560 - 566
SICI:
0959-440X(200110)11:5<560:DMOPBE>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
TYROSINE-PHOSPHATASE 1B; LIGAND-BINDING; ASPARTIC PROTEASE; SH2 DOMAIN; INHIBITOR; AFFINITY; ACID; DEPENDENCE; DISSECTION; DESIGN;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Leavitt, S Johns Hopkins Univ, Dept Biol, Baltimore, MD 21218 USA Johns Hopkins Univ Baltimore MD USA 21218 timore, MD 21218 USA
Citazione:
S. Leavitt e E. Freire, "Direct measurement of protein binding energetics by isothermal titration calorimetry", CURR OP STR, 11(5), 2001, pp. 560-566

Abstract

Of all the techniques that are currently available to measure binding, isothermal titration calorimetry is the only one capable of measuring not onlythe magnitude of the binding affinity but also the magnitude of the two thermodynamic terms that define the binding affinity: the enthalpy (DeltaH) and entropy (DeltaS) changes. Recent advances in instrumentation have facilitated the development of experimental designs that permit the direct measurement of arbitrarily high binding affinities, the coupling of binding to protonation/deprotonation processes and the analysis of binding thermodynamics in terms of structural parameters. Because isothermal titration calorimetry has the capability to measure different energetic contributions to the binding affinity, it provides a unique bridge between computational and experimental analysis. As such, it is increasingly becoming an essential tool in molecular design.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 23:51:49