Yang C H, Brown J N, Kopple K D
Int J Pept Protein Res. 1979 Jul;14(1):12-20. doi: 10.1111/j.1399-3011.1979.tb01915.x.
The structures of 37 peptide crystals, containing 78 water-peptide hydrogen bonds and 77 other hydrogen bonds involving water, were surveyed to identify the geometry of peptide backbone hydration. In the sample, hydration of peptide carbonyl occurred more frequently than hydration of peptide N--H. The most probable value of the C'=O ... O water angle was near 138 degrees, considerably greater than the 120 degrees to the axis of a lone electron pair on the carbonyl oxygen. Associated water oxygens tended to be in the plane of the peptide bond, bui--H and Ci+1=O atoms, was common in glycine-containing cyclic hexapeptides. The distribution of angles between two hydrogen bonds at a single water molecule, as defined by the three nonhydrogen atoms involved, was centered near the tetrahedral angle.
对37个肽晶体的结构进行了研究，这些晶体包含78个水 - 肽氢键和77个涉及水的其他氢键，以确定肽主链水化的几何结构。在该样本中，肽羰基的水化比肽N - H的水化更频繁。C'=O...O水角的最可能值接近138度，远大于羰基氧上孤电子对轴的120度。相关的水氧原子倾向于位于肽键平面内，但是 - H和Ci + 1 = O原子在含甘氨酸的环状六肽中很常见。由涉及的三个非氢原子定义的单个水分子处两个氢键之间的角度分布集中在四面体角附近。
