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.
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},
}
Downloads: 0
{"_id":"N4rYqK45TPTzwbY7o","bibbaseid":"rienstra-tuckerkellogg-jaroniec-hohwy-reif-mcmahon-tidor-lozanoprez-etal-denovodeterminationofpeptidestructurewithsolidstatemagicanglespinningnmrspectroscopy-2002","author_short":["Rienstra, C. M","Tucker-Kellogg, L.","Jaroniec, C. P","Hohwy, M.","Reif, B.","McMahon, M. T","Tidor, B.","Lozano-Pérez, T.","Griffin, R. G"],"bibdata":{"bibtype":"article","type":"article","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":[{"propositions":[],"lastnames":["Rienstra"],"firstnames":["Chad","M"],"suffixes":[]},{"propositions":[],"lastnames":["Tucker-Kellogg"],"firstnames":["Lisa"],"suffixes":[]},{"propositions":[],"lastnames":["Jaroniec"],"firstnames":["Christopher","P"],"suffixes":[]},{"propositions":[],"lastnames":["Hohwy"],"firstnames":["Morten"],"suffixes":[]},{"propositions":[],"lastnames":["Reif"],"firstnames":["Bernd"],"suffixes":[]},{"propositions":[],"lastnames":["McMahon"],"firstnames":["Michael","T"],"suffixes":[]},{"propositions":[],"lastnames":["Tidor"],"firstnames":["Bruce"],"suffixes":[]},{"propositions":[],"lastnames":["Lozano-Pérez"],"firstnames":["Tomas"],"suffixes":[]},{"propositions":[],"lastnames":["Griffin"],"firstnames":["Robert","G"],"suffixes":[]}],"month":"August","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","bibtex":"@article{Rienstra2002,\n\ttitle = {De novo determination of peptide structure with solid-state magic-angle spinning {NMR} spectroscopy.},\n\tvolume = {99},\n\tissn = {0027-8424},\n\turl = {http://www.pnas.org/content/99/16/10260.full},\n\tdoi = {10.1073/pnas.152346599},\n\tabstract = {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.},\n\tnumber = {16},\n\tjournal = {Proceedings of the National Academy of Sciences of the United States of America},\n\tauthor = {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},\n\tmonth = aug,\n\tyear = {2002},\n\tpmid = {12149447},\n\tkeywords = {\\#nosource, Biomolecular, Biomolecular: methods, N-Formylmethionine Leucyl-Phenylalanine, N-Formylmethionine Leucyl-Phenylalanine: chemistry, Nuclear Magnetic Resonance, Peptides, Peptides: chemistry, Protein Structure, Tertiary},\n\tpages = {10260--10265},\n}\n\n\n\n","author_short":["Rienstra, C. M","Tucker-Kellogg, L.","Jaroniec, C. P","Hohwy, M.","Reif, B.","McMahon, M. T","Tidor, B.","Lozano-Pérez, T.","Griffin, R. G"],"key":"Rienstra2002","id":"Rienstra2002","bibbaseid":"rienstra-tuckerkellogg-jaroniec-hohwy-reif-mcmahon-tidor-lozanoprez-etal-denovodeterminationofpeptidestructurewithsolidstatemagicanglespinningnmrspectroscopy-2002","role":"author","urls":{"Paper":"http://www.pnas.org/content/99/16/10260.full"},"keyword":["#nosource","Biomolecular","Biomolecular: methods","N-Formylmethionine Leucyl-Phenylalanine","N-Formylmethionine Leucyl-Phenylalanine: chemistry","Nuclear Magnetic Resonance","Peptides","Peptides: chemistry","Protein Structure","Tertiary"],"metadata":{"authorlinks":{}},"html":""},"bibtype":"article","biburl":"https://bibbase.org/zotero/subhradip.paul","dataSources":["epdxi2MtNPwoQCL4d"],"keywords":["#nosource","biomolecular","biomolecular: methods","n-formylmethionine leucyl-phenylalanine","n-formylmethionine leucyl-phenylalanine: chemistry","nuclear magnetic resonance","peptides","peptides: chemistry","protein structure","tertiary"],"search_terms":["novo","determination","peptide","structure","solid","state","magic","angle","spinning","nmr","spectroscopy","rienstra","tucker-kellogg","jaroniec","hohwy","reif","mcmahon","tidor","lozano-pérez","griffin"],"title":"De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy.","year":2002}