De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy. Rienstra, C. M, Tucker-Kellogg, L., Jaroniec, C. P, Hohwy, M., Reif, B., McMahon, M. T, Tidor, B., Lozano-Pérez, T., & Griffin, R. G Proceedings of the National Academy of Sciences of the United States of America, 99(16):10260–10265, August, 2002. ![De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy. [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex 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.
@article{Rienstra2002,
title = {De novo determination of peptide structure with solid-state magic-angle spinning {NMR} spectroscopy.},
volume = {99},
issn = {0027-8424},
url = {http://www.pnas.org/content/99/16/10260.full},
doi = {10.1073/pnas.152346599},
abstract = {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.},
number = {16},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
author = {Rienstra, Chad M and Tucker-Kellogg, Lisa and Jaroniec, Christopher P and Hohwy, Morten and Reif, Bernd and McMahon, Michael T and Tidor, Bruce and Lozano-Pérez, Tomas and Griffin, Robert G},
month = aug,
year = {2002},
pmid = {12149447},
keywords = {\#nosource, Biomolecular, Biomolecular: methods, N-Formylmethionine Leucyl-Phenylalanine, N-Formylmethionine Leucyl-Phenylalanine: chemistry, Nuclear Magnetic Resonance, Peptides, Peptides: chemistry, Protein Structure, Tertiary},
pages = {10260--10265},
}
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