H-NMR assignments and conformational studies of melanin concentrating hormone in water using two-dimensional NMR

Terry O Matsunaga, Catherine A. Gehrig, Victor J Hruby

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

The question of a structural link between MCH and MSH has led us to study the conformation of MCH in solution by nmr spectroscopy. Peptides or linear fragments of proteins of this size and magnitude are not as disordered as originally believed, and actually can have a good deal of relatively stable secondary structure. The presence of a cyclic disulfide ring in MCH enhances the probability of a structurally defined peptide. Using recent advances in two-dimensional (2D) methodology including phase-sensitive nuclear Overhauser enhanced spectroscopy (NOESY), and phase-sensitive correlated spectroscopy (COSY), we have been able to ascertain considerable conformational information about MCH.

Original languageEnglish (US)
Pages (from-to)1291-1295
Number of pages5
JournalBiopolymers - Peptide Science Section
Volume30
Issue number13-14
StatePublished - 1990

Fingerprint

Melanin
Hormones
Spectrum Analysis
Nuclear magnetic resonance
Spectroscopy
Peptides
Water
Melanocyte-Stimulating Hormones
Disulfides
Conformations
Proteins
melanin-concentrating hormone

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics

Cite this

H-NMR assignments and conformational studies of melanin concentrating hormone in water using two-dimensional NMR. / Matsunaga, Terry O; Gehrig, Catherine A.; Hruby, Victor J.

In: Biopolymers - Peptide Science Section, Vol. 30, No. 13-14, 1990, p. 1291-1295.

Research output: Contribution to journalArticle

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