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 13C-15N distances and 18 torsion angle constraints (on 10 angles), recorded from uniformly 13C, 15N- and 15N-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.
|Original language||English (US)|
|Number of pages||6|
|Journal||Proceedings of the National Academy of Sciences of the United States of America|
|State||Published - Aug 2002|
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