Rienstra Chad M, Tucker-Kellogg Lisa, Jaroniec Christopher P, Hohwy Morten, Reif Bernd, McMahon Michael T, Tidor Bruce, Lozano-Pérez Tomas, Griffin Robert G
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Proc Natl Acad Sci U S A. 2002 Aug 6;99(16):10260-5. doi: 10.1073/pnas.152346599. Epub 2002 Jul 29.
The three-dimensional structure of the chemotactic peptide N-formyl-l-Met-l-Leu-l-Phe-OH was determined by using solid-state NMR (SSNMR). The set of SSNMR data consisted of 16 (13)C-(15)N distances and 18 torsion angle constraints (on 10 angles), recorded from uniformly (13)C,(15)N- and (15)N-labeled samples. The peptide's structure was calculated by means of simulated annealing and a newly developed protocol that ensures that all of conformational space, consistent with the structural constraints, is searched completely. The result is a high-quality structure of a molecule that has thus far not been amenable to single-crystal diffraction studies. The extensions of the SSNMR techniques and computational methods to larger systems appear promising.
通过使用固态核磁共振（SSNMR）确定了趋化肽N-甲酰基-L-蛋氨酸-L-亮氨酸-L-苯丙氨酸-OH的三维结构。该组SSNMR数据由16个（13）C-（15）N距离和18个扭转角约束（关于10个角度）组成，这些数据来自均匀（13）C、（15）N和（15）N标记的样品。通过模拟退火和一种新开发的协议计算肽的结构，该协议确保完全搜索与结构约束一致的所有构象空间。结果是得到了一个迄今为止不适用于单晶衍射研究的分子的高质量结构。将SSNMR技术和计算方法扩展到更大的系统似乎很有前景。
