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

doi:10.1016/0141-8130(86)90017-6

International Journal of Biological Macromolecules

Volume 8, Issue 3, June 1986, Pages 149-152

https://doi.org/10.1016/0141-8130(86)90017-6 Get rights and content

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 C^αH^α 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.

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Solution- and solid-state c.d. spectra, as well as surface energetics values, were collected for a series of peptides derived from human salivary proline-rich glycoprotein (PRG). The acronyms and sequences for these peptides are as follows: PRG9-2 = NH₂-G(1)-P(2)-CONH₂, PRG9-3 = NH₂-G(1)-P(2)-P(3)-CONH₂, PRG9-4 = NH₂-G(1)-P(2)-P(3)-P(4)-CONH₂, PRG9-5 = NH₂-G(1)-P(2)-P(3)-P(4)-H(5)-CONH₂, PRG9-6 = NH₂-G(1)-P(2)-P(3)-P(4)-H(5)-P(6)-CONH₂, PRG9-7 = NH₂-G(1)-P(2)-P(3)-P(4)-H(5)-P(6)-G(7)-CONH₂, PRG9-8 = NH₂-G(1)-P(2)-P(3)-P(4)-H(5)-P(6)-G(7)-K(8)-CONH₂, and PRG9-9 = NH₂-G(1)-P(2)-P(3)-P(4)-H(5)-P(6)-G(7)-K(8)-P(9)-CONH₂. The presence of stable poly-l-proline II-like ‘mini’ helices in the solution state was found to be dependent on peptide chain length, pH, salt, and organic solvent type. Other conformational features such as kinks and β-/γ-turns were also found in the larger peptides. Solid-state peptide conformations were not necessarily related to their solution-state counterparts. Poly-l-proline II-like ‘mini’ helices, kinks, and β-/γ-turns were similarly found in the various substrate-bound PRG9 peptides. Surface energetics parameters suggested specific orientations for PRG9 peptides and their constituent acids and homopolymers.
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Dynamics of a proline-rich glycoprotein from human parotid saliva: a 360-MHz proton nuclear magnetic resonance investigation

Abstract

Biochim. Biophys. Acta

J. Biol. Chem.

Biochem. Biophys. Res. Commun.

Biochim. Biophys. Acta

J. Magn. Reson.

J. Magn. Reson.

J. Magn. Reson.

Adv. Carb. Chem. Biochem.

J. Magn. Reson.

Int. J. Pept. Proteins Res.

J. Biol. Chem.

Int. J. Pept. Protein Res.

J. Dent. Res.

J. Periodont.