1q7o
From Proteopedia
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[[Image:1q7o.jpg|left|200px]] | [[Image:1q7o.jpg|left|200px]] | ||
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'''Determination of f-MLF-OH Peptide Structure with solid-state magic-angle spinning NMR Spectroscopy''' | '''Determination of f-MLF-OH Peptide Structure with solid-state magic-angle spinning NMR Spectroscopy''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q7O OCA]. | |
==Reference== | ==Reference== | ||
De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy., Rienstra CM, Tucker-Kellogg L, Jaroniec CP, Hohwy M, Reif B, McMahon MT, Tidor B, Lozano-Perez T, Griffin RG, Proc Natl Acad Sci U S A. 2002 Aug 6;99(16):10260-5. Epub 2002 Jul 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12149447 12149447] | De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy., Rienstra CM, Tucker-Kellogg L, Jaroniec CP, Hohwy M, Reif B, McMahon MT, Tidor B, Lozano-Perez T, Griffin RG, Proc Natl Acad Sci U S A. 2002 Aug 6;99(16):10260-5. Epub 2002 Jul 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12149447 12149447] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Griffin, R G.]] | [[Category: Griffin, R G.]] | ||
[[Category: Hohwy, M.]] | [[Category: Hohwy, M.]] | ||
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[[Category: Tidor, B.]] | [[Category: Tidor, B.]] | ||
[[Category: Tucker-Kellogg, L.]] | [[Category: Tucker-Kellogg, L.]] | ||
| - | [[Category: | + | [[Category: Chemotactic peptide]] |
| - | [[Category: | + | [[Category: Mlf]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:58:13 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 02:58, 3 May 2008
Determination of f-MLF-OH Peptide Structure with solid-state magic-angle spinning NMR Spectroscopy
Overview
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.
About this Structure
Full crystallographic information is available from OCA.
Reference
De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy., Rienstra CM, Tucker-Kellogg L, Jaroniec CP, Hohwy M, Reif B, McMahon MT, Tidor B, Lozano-Perez T, Griffin RG, Proc Natl Acad Sci U S A. 2002 Aug 6;99(16):10260-5. Epub 2002 Jul 29. PMID:12149447 Page seeded by OCA on Sat May 3 05:58:13 2008
