COUPLING OF LOCAL FOLDING TO SITE-SPECIFIC BINDING OF PROTEINS TO DNA
COUPLING OF LOCAL FOLDING TO SITE-SPECIFIC BINDING OF PROTEINS TO DNA
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DOI：
10.1126/science.8303294
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发表时间：
1994-02-11
期刊：
影响因子：
56.9
通讯作者：
RECORD, MT
中科院分区：
文献类型：
--
作者：
SPOLAR, RS;RECORD, MT
热力学研究已经证明了在位点特异性蛋白质-DNA识别中大的负热容量变化（Δ LTAC（Δ STAC）度）的核心重要性。大的负DELTAC（ashtag）度和蛋白质-配体和蛋白质-DNA复合的熵变的解剖提供了一个热力学签名识别过程中，局部折叠耦合到结合。从该分析中获得的折叠结合的残基数量的估计值与结构数据一致。结构比较表明，这些局部折叠转换创建蛋白质-DNA界面的关键部分。能量的影响，这种“诱导适合”模型的DNA位点识别被认为是。
Thermodynamic studies have demonstrated the central importance of a large negative heat capacity change (DELTAC(assoc)degrees) in site-specific protein-DNA recognition. Dissection of the large negative DELTAC(assoc)degrees and the entropy change of protein-ligand and protein-DNA complexation provide a thermodynamic signature identifying processes in which local folding is coupled to binding. Estimates of the number of residues that fold on binding obtained from this analysis agree with structural data. Structural comparisons indicate that these local folding transitions create key parts of the protein-DNA interface. The energetic implications of this ''induced fit'' model for DNA site recognition are considered.