Two-dimensional differential scanning calorimetry: simultaneous resolution of intrinsic protein structural energetics and ligand binding interactions by global linkage analysis.
Two-dimensional differential scanning calorimetry: simultaneous resolution of intrinsic protein structural energetics and ligand binding interactions by global linkage analysis.
复制标题
二维差示扫描量热法：通过全局连锁分析同时解析内在蛋白质结构能量和配体结合相互作用。
DOI：
10.1016/0003-2697(92)90311-t
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发表时间：
1992
影响因子：
2.9
通讯作者：
Freire,E
中科院分区：
文献类型：
--
作者：
Straume,M;Freire,E
蛋白质二维热稳定表面的设计和分析的一般理论发展。这些表面是从不同浓度的相互作用配体获得的多个过剩热容曲线（ΔCp Δ vsT）中产生的。采用统计热力学模型，在全局连锁分析中同时解决了蛋白质内在稳定性和蛋白质-配体相互作用的能量学问题。这种形式主义允许分辨率的内在蛋白质折叠展开参数（焓，熵，和热容量的变化）以及配体相互作用参数（结合化学计量，焓，熵，和热容量的变化）。该理论已被应用于核糖核酸酶A及其与胞苷-2 ′-单磷酸相互作用的情况。通过这种方法获得的热力学参数的准确性比较的误差范围内的那些参数，可以通过直接测量。
A general theoretical development for the design and analysis of two-dimensional thermal stability surfaces of proteins is presented. The surfaces are generated from multiple excess heat capacity profiles (〈ΔCp〉 vsT) obtained at varying concentrations of an interacting ligand. The energetics of both the intrinsic protein stability and the protein-ligand interaction are simultaneously resolved by employing statistical thermodynamic models in global linkage analysis. This formalism allows resolution of the intrinsic protein folding-unfolding parameters (enthalpy, entropy, and heat capacity changes) as well as the ligand interaction parameters (binding stoichiometry, enthalpy, entropy, and heat capacity changes). The theory has been applied to the case of ribonuclease A and its interaction with cytidine-2′-monophosphate. The accuracy of the thermodynamic parameters obtained by this approach compares within error with those parameters that can be obtained by direct measurements.