Karle I L, Awasthi S K, Balaram P
Laboratory for the Structure of Matter, Naval Research Laboratory, Washington, DC 20375-5341, USA.
Proc Natl Acad Sci U S A. 1996 Aug 6;93(16):8189-93. doi: 10.1073/pnas.93.16.8189.
Beta-hairpin structures have been crystallographically characterized only in very short acyclic peptides, in contrast to helices. The structure of the designed beta-hairpin, t-butoxycarbonyl-Leu-Val-Val-D-Pro-Gly-Leu-Val-Val-OMe in crystals is described. The two independent molecules of the octapeptide fold into almost ideal beta-hairpin conformations with the central D-Pro-Gly segment adopting a Type II' beta-turn conformation. The definitive characterization of a beta-hairpin has implications for de novo peptide and protein design, particularly for the development of three- and four-stranded beta-sheets.
与螺旋结构不同，β-发夹结构仅在非常短的无环肽中通过晶体学进行了表征。本文描述了设计的β-发夹结构——叔丁氧羰基-Leu-Val-Val-D-Pro-Gly-Leu-Val-Val-OMe在晶体中的结构。八肽的两个独立分子折叠成几乎理想的β-发夹构象，中心的D-Pro-Gly片段采用II'型β-转角构象。β-发夹结构的确切表征对从头肽和蛋白质设计具有重要意义，特别是对于三链和四链β-折叠片层的开发。
