Do all backbone polar groups in proteins form hydrogen bonds?
Do all backbone polar groups in proteins form hydrogen bonds?
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DOI：
10.1110/ps.051454805
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发表时间：
2005-07-01
期刊：
影响因子：
8
通讯作者：
Rose, GD
中科院分区：
文献类型：
--
作者：
Fleming, PJ;Rose, GD
来自蛋白质和肽的证据支持肽内氢键稳定蛋白质折叠形式的结论。有趣的是，来自小分子的证据支持相反的结论，即肽内氢键不如肽-水氢键有利。一个相关的问题--在比较肽-肽和肽-水氢键的争论中经常被忽略--涉及到一个未满足的氢键的能量消耗。在这里，实验和理论一致认为，打破氢键的成本在5和6千卡/摩尔之间。因此，在蛋白质中发现未满足的氢键的可能性是微不足道的。这一认识为评价蛋白质构象建立了一个强有力的规则。
Evidence from proteins and peptides supports the conclusion that intrapeptide hydrogen bonds stabilize the folded form of proteins. Paradoxically, evidence from small molecules supports the opposite conclusion, that intrapeptide hydrogen bonds are less favorable than peptide-water hydrogen bonds. A related issue-often lost in this debate about comparing peptide-peptide to peptide-water hydrogen bonds-involves the energetic cost of an unsatisfied hydrogen bond. Here, experiment and theory agree that breaking a hydrogen bond costs between 5 and 6 kcal/mol. Accordingly, the likelihood of finding an unsatisfied hydrogen bond in a protein is insignificant. This realization establishes a powerful rule for evaluating protein conformations.