Published in

National Academy of Sciences, Proceedings of the National Academy of Sciences, 16(99), p. 10260-10265, 2002

DOI: 10.1073/pnas.152346599

Links

Tools

Export citation

Search in Google Scholar

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

Journal article published in 2002 by Chad M. Rienstra, Lisa Tucker-Kellogg ORCID, Christopher P. Jaroniec, Morten Hohwy, Bernd Reif ORCID, Michael T. McMahon, Bruce Tidor, Tomás Lozano-Pérez, Robert G. Griffin
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

Full text: Download

Red circle
Preprint: archiving forbidden
Green circle
Postprint: archiving allowed
Upload
Red circle
Published version: archiving forbidden
Policy details
Data provided by SHERPA/RoMEO

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.