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 language | English |
|---|---|
| Pages (from-to) | 149-152 |
| Number of pages | 4 |
| Journal | International Journal of Biological Macromolecules |
| Volume | 8 |
| Issue number | 3 |
| DOIs | |
| State | Published - Jun 1986 |
Keywords
- Glycoprotein
- hydrogen-deuterium exchage
- nuclear magnetic resonance spectroscopy
- saliva
- spin-lattice relaxation
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