Structural highlights
Publication Abstract from PubMedThe 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. De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy.,Rienstra CM, Tucker-Kellogg L, Jaroniec CP, Hohwy M, Reif B, McMahon MT, Tidor B, Lozano-Perez T, Griffin RG Proc Natl Acad Sci U S A. 2002 Aug 6;99(16):10260-5. Epub 2002 Jul 29. PMID:12149447[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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