Nmr and molecular modeling investigations of the neuropeptide substance P in the presence of 15 mM sodium dodecyl sulfate micelles

John K. Young, Rickey P. Hicks, Rickey Paige Hicks

Research output: Contribution to journalArticle

66 Scopus citations

Abstract

To better understand the structural basis of the biological activity of the neuropeptide substance P SP; (Arg‐Pro‐Lys‐Pro‐Gln‐Gln‐Phe‐Phe‐Gly‐Leu‐Met‐NH2), two‐dimensional nmr spectroscopy experiments and simulated annealing calculations were used to investigate the conformation adopted in the presence of the membrane model system sodium dodecyl sulfate. It was determined that SP in the presence of SDS micelles undergoes a conformational equilibrium between an α‐ and a 310‐helix involving the midregion (Pro4‐Gln5‐Gln6‐Phe7‐Phe8) of the peptide. The C‐terminus adopts an extended conformation while the N‐terminus remains quite flexible. The conformation adopted by SP in the presence of SDS micelles yields a structure that is consistent with the model of a neurokinin‐1 selective ligand proposed by Convert. © 1994 John Wiley & Sons, Inc.

Original languageEnglish (US)
Pages (from-to)1449-1462
Number of pages14
JournalBiopolymers
Volume34
Issue number11
DOIs
StatePublished - Jan 1 1994

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry

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