TY - JOUR
T1 - Direct measurement of protein binding energetics by isothermal titration calorimetry
AU - Leavitt, Stephanie
AU - Freire, Ernesto
N1 - Funding Information:
This work was supported by grants from the National Institutes of Health GM51362 and GM57144, and the National Science Foundation MCB-9816661.
PY - 2001/9/1
Y1 - 2001/9/1
N2 - Of all the techniques that are currently available to measure binding, isothermal titration calorimetry is the only one capable of measuring not only the magnitude of the binding affinity but also the magnitude of the two thermodynamic terms that define the binding affinity: the enthalpy (ΔH) and entropy (ΔS) 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.
AB - Of all the techniques that are currently available to measure binding, isothermal titration calorimetry is the only one capable of measuring not only the magnitude of the binding affinity but also the magnitude of the two thermodynamic terms that define the binding affinity: the enthalpy (ΔH) and entropy (ΔS) 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.
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U2 - 10.1016/S0959-440X(00)00248-7
DO - 10.1016/S0959-440X(00)00248-7
M3 - Review article
C2 - 11785756
AN - SCOPUS:0035442411
SN - 0959-440X
VL - 11
SP - 560
EP - 566
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 5
ER -