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. Author manuscript; available in PMC: 2011 Oct 1.
Published in final edited form as: Curr Opin Struct Biol. 2010 Oct 1;20(5):598–605. doi: 10.1016/j.sbi.2010.09.001

Table 1.

Summary of capabilities of calorimeters for measuring binding reactions. Ability to be used for indicated application is based on published data demonstrating measurement of the thermodynamic parameters indicated. Kd is the equilibrium dissociation constant, ΔH is the binding enthalpy, n is the stoichiometry coefficient, and ΔS is the binding entropy.

Calorimeter Configuration Availability Application
Thermodynamic characterization (Kd, ΔH, n, ΔS) Screen by Kd Screen by ΔH
iTC200 (Microcal) and Nano ITC Low Volume (TA Instruments) [14**,4143] ~200 μl chamber with stir paddle on spinning injection syringe
Thermopile sensors
(see online supplement for more detailed information)
commercial instruments Broad range of affinities:
20 μM < Kd < ~2 mM for low-C titrations (cannot determine n)
5 nM <Kd < 50 μM for direct titrations
~50 pM <Kd < 10 nM for competitive displacement titrations
Low throughput (50/day max) yes
Enthalpy array [26,27**,28*] Open thermally isolated surface, 500 nl reaction, electrostatic drop merging, magnetic mixing
Thermistor sensors
research instrument Limited range of affinities (Kd>10−5 M) - yes, higher throughput
[31] Closed 10 μl chamber, 5 μl/min flow
Thermopile sensors
research instrument - - One component immobilized