Department of Physiology and Neuroscience and Zilkha Neurogenetic Institute, Keck School of Medicine, University of Southern California, Los Angeles, CA, USA.
Methods Mol Biol. 2021;2302:69-79. doi: 10.1007/978-1-0716-1394-8_5.
The ability to quantify protein-protein interactions without adding labels to protein has made isothermal titration calorimetry (ITC) a preferred technique to study proteins in aqueous solution. Here, we describe the application of ITC to the study of protein-protein interactions in membrane mimics using the association of integrin αIIb and β3 transmembrane domains in phospholipid bicelles as an example. A higher conceptual and experimental effort compared to water-soluble proteins is required for membrane proteins and rewarded with rare thermodynamic insight into this central class of proteins.
无需对蛋白质进行标记即可定量蛋白质-蛋白质相互作用的能力使等温滴定量热法（ITC）成为研究水溶液中蛋白质的首选技术。在这里，我们将描述 ITC 在使用磷脂双体中的整合素 αIIb 和 β3 跨膜结构域的缔合作为示例在膜模拟物中研究蛋白质-蛋白质相互作用的应用。与水溶性蛋白质相比，膜蛋白需要更高的概念和实验努力，并获得对这类核心蛋白质的罕见热力学见解。
