1Q7O

Determination of f-MLF-OH Peptide Structure with solid-state magic-angle spinning NMR Spectroscopy

Summary for 1Q7O

• Entry DOI: 10.2210/pdb1q7o/pdb
• NMR Information: BMRB: 5934
• Descriptor: chemotactic peptide (1 entity in total)
• Functional Keywords: mlf, chemotactic peptide, de novo protein
• Total number of polymer chains: 1
• Total formula weight: 453.55

Authors

Rienstra, C.M.,Tucker-Kellogg, L.,Jaroniec, C.P.,Hohwy, M.,Reif, B.,McMahon, M.T.,Tidor, B.,Lozano-Perez, T.,Griffin, R.G. (deposition date: 2003-08-19, release date: 2003-09-09, Last modification date: 2022-03-02)

Primary citation

Rienstra, C.M.,Tucker-Kellogg, L.,Jaroniec, C.P.,Hohwy, M.,Reif, B.,McMahon, M.T.,Tidor, B.,Lozano-Perez, T.,Griffin, R.G.
De novo determination of peptide structure with solid-state magic-angle spinning NMR Spectroscopy
Proc.Natl.Acad.Sci.USA, 99:10260-10265, 2002

PubMed 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.

PubMed: 12149447
DOI: 10.1073/pnas.152346599

Experimental method

SOLID-STATE NMR