MRC Laboratory of Molecular Biology, Cambridge, UK.
Methods Mol Biol. 2021;2263:135-159. doi: 10.1007/978-1-0716-1197-5_5.
Calorimetry is a classical biophysical method that by definition measures heat. In isothermal titration calorimetry (ITC), the heat is the result of titrating interacting components together and allows direct determination of the thermodynamics for this process. The measured heat reflects the enthalpy change (ΔH), and the prospect of determining this in biological systems where high-resolution structural information is available has led to the possibility of rational thermodynamics-guided design of ligands. Although there are limitations to this approach due to the participation of solvent in the thermodynamics, ITC has become an established technique in many labs providing a valuable tool with which to quantify protein-protein interactions. With careful use, ITC can also provide additional insights into the binding process or be used in increasingly complex systems and where interaction is coupled to other molecular events.
量热法是一种经典的生物物理方法，根据定义，它测量热量。在等温滴定量热法（ITC）中，热量是滴定相互作用的成分的结果，允许直接确定该过程的热力学。测量的热量反映了焓变（ΔH），并且在具有高分辨率结构信息的生物系统中确定这一点的可能性导致了合理的热力学指导配体设计的可能性。尽管由于溶剂参与热力学而存在一些限制，但 ITC 已成为许多实验室中的一种既定技术，为量化蛋白质-蛋白质相互作用提供了有价值的工具。通过谨慎使用，ITC 还可以提供有关结合过程的更多见解，或者用于越来越复杂的系统和相互作用与其他分子事件偶联的系统。
