De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy Export

@article{citeulike:1512750, abstract = {10.1073/pnas.152346599 The three-dimensional structure of the chemotactic peptide formyl--Met--Leu--Phe-OH was determined by using solid-state NMR (SSNMR). The set of SSNMR data consisted of 16 C–N distances and 18 torsion angle constraints (on 10 angles), recorded from uniformly C,N- and 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.}, 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-P\'{e}rez, Tom\'{a}s and Griffin, Robert G.}, citeulike-article-id = {1512750}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.152346599}, citeulike-linkout-1 = {http://www.pnas.org/content/99/16/10260.abstract}, citeulike-linkout-2 = {http://www.pnas.org/content/99/16/10260.full.pdf}, citeulike-linkout-3 = {http://www.pnas.org/cgi/content/abstract/99/16/10260}, citeulike-linkout-4 = {http://view.ncbi.nlm.nih.gov/pubmed/12149447}, citeulike-linkout-5 = {http://www.hubmed.org/display.cgi?uids=12149447}, day = {6}, doi = {10.1073/pnas.152346599}, journal = {Proceedings of the National Academy of Sciences of the United States of America}, keywords = {crystallography, dynamics, nmr, protein}, month = {August}, number = {16}, pages = {10260--10265}, posted-at = {2009-07-24 20:07:25}, priority = {2}, title = {De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy}, url = {http://dx.doi.org/10.1073/pnas.152346599}, volume = {99}, year = {2002} }

TY - JOUR ID - citeulike:1512750 L3 - citeulike-article-id:1512750 N2 - 10.1073/pnas.152346599 The three-dimensional structure of the chemotactic peptide formyl--Met--Leu--Phe-OH was determined by using solid-state NMR (SSNMR). The set of SSNMR data consisted of 16 C–N distances and 18 torsion angle constraints (on 10 angles), recorded from uniformly C,N- and 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. IS - 16 JF - Proceedings of the National Academy of Sciences of the United States of America EP - 10265 TI - De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy VL - 99 SP - 10260 KW - crystallography KW - dynamics KW - nmr KW - protein AU - Rienstra, Chad AU - Tucker-Kellogg, Lisa AU - Jaroniec, Christopher AU - Hohwy, Morten AU - Reif, Bernd AU - Mcmahon, Michael AU - Tidor, Bruce AU - Lozano-Pérez, Tomás AU - Griffin, Robert PY - 2002/08/06/ UR - http://dx.doi.org/10.1073/pnas.152346599 ER -