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jjoonathan
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Isothermal Titration Calorimetry measures the enthalpy of (e.g.) protein binding by measuring the amount of heat that must be added/removed to a solution in order to perfectly balance the heat generated/released by the gradual introduction of a protein's binding partner. My understanding is that the experiment operates under constant (well, *almost* constant) temperature and pressure. But don't those conditions (constant T, P) mean that ΔG equals the heat generated/released by binding, as opposed to ΔH? How do we know we should use ΔH instead?
Some references:
[1] http://antisensescienceblog.wordpre...plained-isothermal-titration-calorimetry-itc/
[2] http://www.uic.edu/orgs/ctrstbio/manuals/leavitt.pdf
Some references:
[1] http://antisensescienceblog.wordpre...plained-isothermal-titration-calorimetry-itc/
[2] http://www.uic.edu/orgs/ctrstbio/manuals/leavitt.pdf
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