Isothermal Titration Calorimetry of Membrane Proteins.

Isothermal Titration Calorimetry of Membrane Proteins.
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膜蛋白的等温滴定量热法。

DOI:
10.1007/978-1-0716-1394-8_5
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发表时间:
2021
期刊:
Methods in molecular biology (Clifton, N.J.)
影响因子:
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通讯作者:
Ulmer,TobiasS
Ulmer,TobiasS
中科院分区:
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文献类型:
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作者:
Vu,HanN;Situ,AlanJ;Ulmer,TobiasS

文献摘要

相似文献

等温滴定量热法(ITC)能够在不添加标记的情况下定量蛋白质与蛋白质之间的相互作用,这使得它成为研究水溶液中蛋白质的首选技术。本文以整合素αIIb和β3跨膜结构域在磷脂单胞体中的关联为例,描述了ITC在膜模拟物中蛋白质-蛋白质相互作用研究中的应用。与水溶性蛋白质相比,膜蛋白需要更高的概念和实验努力,并且对这类核心蛋白质有罕见的热力学见解。
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.