Hydrogen bonding increases packing density in the protein interior.
Hydrogen bonding increases packing density in the protein interior.
复制标题
氢键增加了蛋白质内部的堆积密度。
作者：
Schell,David;Tsai,Jerry;Scholtz,JMartin;Pace,CNick
氢键和极性基团的埋藏对蛋白质稳定性的贡献是一个有争议的话题。理论研究表明，在蛋白质内部掩埋极性基团不利于蛋白质的稳定性，但实验研究表明，掩埋极性基团，特别是那些氢键，有利于蛋白质的稳定性。理解理论模型没有正确考虑的因素将改进模型，使它们更准确地描述实验结果。已经提出，氢键可能有助于蛋白质稳定性，部分地通过增加蛋白质内部的堆积密度，从而增加货车范德华相互作用对蛋白质稳定性的贡献。为了研究氢键对堆积密度的影响，我们分析了687种晶体结构，并确定了埋置极性基团的体积作为其氢键范围的函数。我们的研究结果表明，形成氢键的肽基团和极性侧链比不形成氢键的相同基团占据更小的体积。例如，其中两个极性基团都是氢键键合的肽基团占据的体积平均比没有氢键键合的肽基团小5.2 μ m。蛋白质2006; 63：278-282.
The contribution of hydrogen bonds and the burial of polar groups to protein stability is a controversial subject. Theoretical studies suggest that burying polar groups in the protein interior makes an unfavorable contribution to the stability, but experimental studies show that burying polar groups, especially those that are hydrogen bonded, contributes favorably to protein stability. Understanding the factors that are not properly accounted for by the theoretical models would improve the models so that they more accurately describe experimental results. It has been suggested that hydrogen bonds may contribute to protein stability, in part, by increasing packing density in the protein interior, and thereby increasing the contribution of van der Waals interactions to protein stability. To investigate the influence of hydrogen bonds on packing density, we analyzed 687 crystal structures and determined the volume of buried polar groups as a function of their extent of hydrogen bonding. Our findings show that peptide groups and polar side chains that form hydrogen bonds occupy a smaller volume than the same groups when they do not form hydrogen bonds. For example, peptide groups in which both polar groups are hydrogen bonded occupy a volume, on average, 5.2 Å3 less than a peptide group that is not hydrogen bonded. Proteins 2006; 63: 278–282.