How similar are protein folding and protein binding nuclei? Examination of vibrational motions of energy hot spots and conserved residues
How similar are protein folding and protein binding nuclei? Examination of vibrational motions of energy hot spots and conserved residues
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DOI：
10.1529/biophysj.104.051342
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发表时间：
2005-03-01
影响因子：
3.4
通讯作者：
Nussinov, R
中科院分区：
文献类型：
--
作者：
Haliloglu, T;Keskin, O;Nussinov, R
蛋白质折叠中结构域之间相互作用的基本物理化学原理与蛋白质分子之间结合的原理相似。在这里，我们表明，保守的残基和实验热点在分子间结合界面重叠的残基，以高频率振动。类似地，在蛋白质核心中发现保守残基和热点，并且也观察到以高频率振动。在这两种情况下，这些残基对稳定性有显著贡献。因此，这些观察证实了结合和折叠是类似过程的命题。在这两个包装起着至关重要的作用，合理化的残基保护和实验丙氨酸扫描热点。我们进一步表明，高频振动残基区分蛋白质结合位点和蛋白质表面的其余部分。
The underlying physico-chemical principles of the interactions between domains in protein folding are similar to those between protein molecules in binding. Here we show that conserved residues and experimental hot spots at intermolecular binding interfaces overlap residues that vibrate with high frequencies. Similarly, conserved residues and hot spots are found in protein cores and are also observed to vibrate with high frequencies. In both cases, these residues contribute significantly to the stability. Hence, these observations validate the proposition that binding and folding are similar processes. In both packing plays a critical role, rationalizing the residue conservation and the experimental alanine scanning hot spots. We further show that high-frequency vibrating residues distinguish between protein binding sites and the remainder of the protein surface.