Heat capacity changes for protein-peptide interactions in the ribonuclease S system.
Heat capacity changes for protein-peptide interactions in the ribonuclease S system.
复制标题
核糖核酸酶 S 系统中蛋白质-肽相互作用的热容变化。
作者：
R. Varadarajan;P. Connelly;J. Sturtevant;F. Richards
胰核糖核酸酶A的两个片段，S-肽（残基1-15）和S-蛋白（残基21-124）的截短形式，联合收割机结合产生催化活性复合物，命名为核糖核酸酶S。我们已经取代了野生型残基Met-13与其他6个疏水残基的大小从丙氨酸到苯丙氨酸，并确定了热力学参数与这些类似物结合的S-蛋白的滴定量热法在温度范围5-25摄氏度。结合的热容量变化（Δ Cp）得到从一个全球性的分析的自由能和结合的温度依赖性。Δ Cp不以任何简单的方式与结合后掩埋的非极性表面积（Δ Anp）相关。
Two fragments of pancreatic ribonuclease A, a truncated version of S-peptide (residues 1-15) and S-protein (residues 21-124), combine to give a catalytically active complex designated ribonuclease S. We have substituted the wild-type residue Met-13 with six other hydrophobic residues ranging in size from alanine to phenylalanine and have determined the thermodynamic parameters associated with binding of these analogues to S-protein by titration calorimetry in the temperature range 5-25 degrees C. The heat capacity change (delta Cp) associated with binding was obtained from a global analysis of the temperature dependences of the free energies and enthalpies of binding. The delta Cp's were not correlated in any simple fashion with the nonpolar surface area (delta Anp) buried upon binding.
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DOI：
10.1073/pnas.86.21.8382
发表时间：
1989-11
影响因子：
11.1
作者：
Ruth S. Spolar;J. Ha;Record Mt
通讯作者：
Ruth S. Spolar;J. Ha;Record Mt
影响因子：
2.9
作者：
LIVINGSTONE, JR;SPOLAR, RS;RECORD, MT
通讯作者：
RECORD, MT
DOI：
10.1073/pnas.83.21.8069
发表时间：
1986-11-01
影响因子：
11.1
作者：
BALDWIN, RL
通讯作者：
BALDWIN, RL
影响因子：
2.9
作者：
WISEMAN, T;WILLISTON, S;LIN, LN
通讯作者：
LIN, LN