Mastropaolo D, Camerman A, Ma L Y, Camerman N
Life Sci. 1987 May 18;40(20):1995-9. doi: 10.1016/0024-3205(87)90289-x.
The structure of a new crystal form of leucine-enkephalin has been determined by X-ray diffraction. There are two independent molecules in the asymmetric unit and both have extended peptide backbone conformations with side-chains arranged alternately above and below the backbone planes. The two pentapeptides are hydrogen-bonded to each other and to other molecules forming an extended antiparallel beta-pleated sheet. The structure differs from that in similar crystals of methionine enkephalin primarily in side-chain orientations and inter-sheet interactions.
亮氨酸脑啡肽新晶型的结构已通过X射线衍射确定。不对称单元中有两个独立的分子，两者都具有延伸的肽主链构象，侧链在主链平面的上方和下方交替排列。这两个五肽彼此之间以及与其他分子形成氢键，构成一个延伸的反平行β折叠片层。该结构与甲硫氨酸脑啡肽类似晶体的结构主要在侧链取向和片层间相互作用方面有所不同。
