Department of Biochemistry, Memorial University of Newfoundland, St. John's, NL, Canada.
J Pept Sci. 2009 Dec;15(12):818-23. doi: 10.1002/psc.1179.
The structure of Peptide T was determined by solution NMR spectroscopy, under strong structure-inducing conditions: 40% hexafluoro-2-propanol aqueous solution at 5 degrees C. Under these conditions it was possible to detect medium-range NOEs for the first time for this peptide. This allowed a much better-defined structure to be determined for Peptide T in comparison with earlier NMR and computational studies. Peptide structures consistent with the experimental restraints were generated using a restrained MD simulation with a full empirical force field. Residues 4-8 of Peptide T take on a well-defined structure with a heavy atom RMSD of 0.78 A. The structure is stabilized by hydrogen bonding to side-chain oxygen atoms of Thr 4 and Thr 8, as well as backbone hydrogen bonding between residues 5 and 7 that forms this region into a classic gamma-turn.
Peptide T 的结构通过溶液 NMR 光谱确定，在强烈的结构诱导条件下：5°C 的 40%六氟异丙醇水溶液。在这些条件下，首次能够检测到该肽的中程 NOE。与早期的 NMR 和计算研究相比，这使得可以为 Peptide T 确定更明确的结构。使用具有完整经验力场的受约束 MD 模拟生成与实验约束一致的肽结构。Peptide T 的 4-8 位残基具有明确的结构，重原子 RMSD 为 0.78A。结构通过与 Thr 4 和 Thr 8 的侧链氧原子的氢键以及形成该区域为经典 γ-转角的残基 5 和 7 之间的骨架氢键稳定。
