Görbitz Carl Henrik, Hartviksen Lars Male
Department of Chemistry, University of Oslo, PO Box 1033 Blindern, N-0315 Oslo, Norway.
Acta Crystallogr C. 2008 Mar;64(Pt 3):o171-6. doi: 10.1107/S0108270108004228. Epub 2008 Feb 23.
The crystal structures of the four dipeptides L-seryl-L-asparagine monohydrate, C(7)H(13)N(3)O(5) x H(2)O, L-seryl-L-tyrosine monohydrate, C(12)H(16)N(2)O(5) x H(2)O, L-tryptophanyl-L-serine monohydrate, C(14)H(17)N(3)O(4) x H(2)O, and L-tyrosyl-L-tryptophan monohydrate, C(20)H(21)N(3)O(4) x H(2)O, are dominated by extensive hydrogen-bonding networks that include cocrystallized solvent water molecules. Side-chain conformations are discussed on the basis of previous observations in dipeptides. These four dipeptide structures greatly expand our knowledge on dipeptides incorporating polar residues such as serine, asparagine, threonine, tyrosine and tryptophan.
四种二肽一水合L-丝氨酰-L-天冬酰胺(C₇H₁₃N₃O₅·H₂O)、一水合L-丝氨酰-L-酪氨酸(C₁₂H₁₆N₂O₅·H₂O)、一水合L-色氨酰-L-丝氨酸(C₁₄H₁₇N₃O₄·H₂O)和一水合L-酪氨酰-L-色氨酸(C₂₀H₂₁N₃O₄·H₂O)的晶体结构主要由广泛的氢键网络构成,其中包括共结晶的溶剂水分子。基于先前对二肽的观察结果讨论了侧链构象。这四种二肽结构极大地扩展了我们对包含极性残基(如丝氨酸、天冬酰胺、苏氨酸、酪氨酸和色氨酸)的二肽的认识。