De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy.
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.
Rienstra
Chad M
CM
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Tucker-Kellogg
Lisa
L
Jaroniec
Christopher P
CP
Hohwy
Morten
M
Reif
Bernd
B
McMahon
Michael T
MT
Tidor
Bruce
B
Lozano-Pérez
Tomas
T
Griffin
Robert G
RG
D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D010455:Peptides / Q000737:chemistry; D017434:Protein Structure, Tertiary
D010455:Peptides; D009240:N-Formylmethionine Leucyl-Phenylalanine