De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy
AUTOR(ES)
Rienstra, Chad M.
FONTE
National Academy of Sciences
RESUMO
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 13C–15N distances and 18 torsion angle constraints (on 10 angles), recorded from uniformly 13C,15N- and 15N-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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=124901Documentos Relacionados
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