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Dynamics of a proline-rich glycoprotein from human parotid saliva: a 360-MHz proton nuclear magnetic resonance investigation

  • SUNY Buffalo

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

The 360-MHz proton n.m.r. spectra of a proline-rich glycoprotein from human parotid saliva (PRG) were obtained in order to analyse spin-lattice relaxation (T1) times and hydrogen-deuterium exchange rates. The (T1) values for the proline ring and bulk peptide backbone CαHα protons were found to be about 0.5 s. The HåD exchange data revealed that only four of the many N-H resonances remained after the first few minutes of exchange. Within 96 h at 12°C most of the remaining peak intensities were gone. These data imply a dynamic conformation with a majority of the backbone free of hydrogen-bonded structures.

Original languageEnglish
Pages (from-to)149-152
Number of pages4
JournalInternational Journal of Biological Macromolecules
Volume8
Issue number3
DOIs
StatePublished - Jun 1986

Keywords

  • Glycoprotein
  • hydrogen-deuterium exchage
  • nuclear magnetic resonance spectroscopy
  • saliva
  • spin-lattice relaxation

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