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

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.

SUBMITTER: Rienstra CM

PROVIDER: S-EPMC124901 | biostudies-literature | 2002 Aug

REPOSITORIES: biostudies-literature

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

Rienstra Chad M CM 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

Proceedings of the National Academy of Sciences of the United States of America 20020729 16

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 constrain ...[more]

PMID: 12149447

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