Fleming Patrick J, Rose George D
T. C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.
Protein Sci. 2005 Jul;14(7):1911-7. doi: 10.1110/ps.051454805. Epub 2005 Jun 3.
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.
肽内氢键稳定了蛋白质的折叠形式。矛盾的是,来自小分子的证据却支持相反的结论,即肽内氢键不如肽与水之间的氢键有利。一个相关问题——在这场关于比较肽-肽氢键与肽-水氢键的争论中常常被忽视——涉及未满足氢键的能量成本。在此,实验和理论一致认为,打破一个氢键的成本在5至6千卡/摩尔之间。因此,在蛋白质中发现未满足氢键的可能性微乎其微。这一认识确立了一条评估蛋白质构象的有力规则。