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Homer RB, Roberts K. Glycoprotein conformation in plant cell walls : Circular dichroism reveals a polyproline II structure. Planta. 1979;146(2):217-22doi: 10.1007/BF00388235.
Homer, R. B., & Roberts, K. (1979). Glycoprotein conformation in plant cell walls : Circular dichroism reveals a polyproline II structure. Planta, 146(2), 217-22. https://doi.org/10.1007/BF00388235
Homer, R B, and Roberts, K. "Glycoprotein conformation in plant cell walls : Circular dichroism reveals a polyproline II structure." Planta vol. 146,2 (1979): 217-22. doi: https://doi.org/10.1007/BF00388235
Homer RB, Roberts K. Glycoprotein conformation in plant cell walls : Circular dichroism reveals a polyproline II structure. Planta. 1979 Jan;146(2):217-22. doi: 10.1007/BF00388235. PMID: 24318062.
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Planta. 1979 Jan;146(2):217-22. doi: 10.1007/BF00388235.

Glycoprotein conformation in plant cell walls : Circular dichroism reveals a polyproline II structure.

Planta

R B Homer, K Roberts

Affiliations

  1. John Innes Institute, Colney Lane, NR4 7UH, Norwich, U.K..

PMID: 24318062 DOI: 10.1007/BF00388235

Abstract

The major structural glycoprotein of the cell wall of Chlamydomonas reinhardii has a protein core, at least 50% of which is in the unusual polyproline II conformation. This has been demonstrated by examining the circular dichroism of the cell wall, its constituent glycoproteins, and thermolysin released wall glycopeptides. One of these glycopeptides, T2, has a high hydroxyproline and sugar content, and possesses upward of 85% polyproline II structure. The main extracellular matrix glycoprotein therefore has a rigid, rod-like structure and the significance of this and its relation to higher plant cell wall glycoproteins is discussed. The unusual conformation appears to confer great stability on the glycoprotein as it is unchanged either by certain denaturing agents or during the transition from protomer to assembled cell wall.

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