Using isothermal titration calorimetry to determine thermodynamic parameters of protein-glycosaminoglycan interactions.
Using isothermal titration calorimetry to determine thermodynamic parameters of protein-glycosaminoglycan interactions.
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DOI：
10.1007/978-1-4939-1714-3_25
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发表时间：
2015
期刊：
影响因子：
--
通讯作者：
Rajarathnam K
中科院分区：
文献类型：
--
作者：
Dutta AK;Rösgen J;Rajarathnam K
现在越来越清楚的是，对生物大分子如何相互识别的完整原子描述不仅需要了解络合物的结构，还需要了解动力学和热力学是如何驱动结合过程的。特别是，对于蛋白质-糖胺多聚糖(GAG)复合体来说，这种知识是缺乏的。等温滴定量热法(ITC)是唯一一种可以从一次实验中提供各种热力学参数--热焓、熵、自由能(结合常数)和化学计量的技术。在这里，我们描述了在进行ITC滴定以获得有意义的蛋白质-GAG相互作用的热力学数据时必须考虑的不同因素。
It has now become increasingly clear that a complete atomic description of how biomacromolecules recognize each other requires knowledge not only of the structures of the complexes but also of how kinetics and thermodynamics drive the binding process. In particular, such knowledge is lacking for protein–glycosaminoglycan (GAG) complexes. Isothermal titration calorimetry (ITC) is the only technique that can provide various thermodynamic parameters—enthalpy, entropy, free energy (binding constant), and stoichiometry—from a single experiment. Here we describe different factors that must be taken into consideration in carrying out ITC titrations to obtain meaningful thermodynamic data of protein–GAG interactions.