TY - JOUR
T1 - Isothermal titration calorimetry.
AU - Velázquez-Campoy, Adrián
AU - Ohtaka, Hiroyasu
AU - Nezami, Azin
AU - Muzammil, Salman
AU - Freire, Ernesto
PY - 2004/9
Y1 - 2004/9
N2 - In the last two decades, isothermal titration calorimetry (ITC) has become the preferred technique to determine the binding energetics of biological processes, including protein-ligand binding, protein-protein binding, DNA-protein binding, protein-carbohydrate binding, protein-lipid binding, and antigen-antibody binding. In this unit several protocols are presented, ranging from the basic ones that are aimed at characterizing binding of moderate affinity to advanced protocols that are aimed at determining very high or very low affinity binding processes. Also, alternate protocols for special cases (homodimeric proteins and unstable proteins) and additional information accessible by ITC (heat capacity and protonation/deprotonation processes coupled to binding) are presented.
AB - In the last two decades, isothermal titration calorimetry (ITC) has become the preferred technique to determine the binding energetics of biological processes, including protein-ligand binding, protein-protein binding, DNA-protein binding, protein-carbohydrate binding, protein-lipid binding, and antigen-antibody binding. In this unit several protocols are presented, ranging from the basic ones that are aimed at characterizing binding of moderate affinity to advanced protocols that are aimed at determining very high or very low affinity binding processes. Also, alternate protocols for special cases (homodimeric proteins and unstable proteins) and additional information accessible by ITC (heat capacity and protonation/deprotonation processes coupled to binding) are presented.
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M3 - Review article
C2 - 18228446
AN - SCOPUS:40549119840
VL - Chapter 17
SP - Unit 17.8
JO - Current Protocols in Cell Biology
JF - Current Protocols in Cell Biology
SN - 1934-2500
ER -