A model for the triple-helical structure of (Pro-Hyp-Gly)10 involving a cis peptide bond and inter-chain hydrogen-bonding to the hydroxyl group of hydroxyproline. Academic Article uri icon

abstract

  • A model for the triple-helical conformation of (Pro-Hyp-Gly)10 has been developed which can account for the recent observation that hydroxyproline contributes to the stability of the triple helix in aqueous solution. Previous structures proposed for (Pro-Gly-Pro)n and collagen were modified to allow the formation of a new inter-chain hydrogen bond between the hydroxyl group of hydroxyproline and the carbonyl group of glycine in an adjacent chain. To create this hydrogen bond, the new model postulates a cis peptide bond between glycine and proline. 1973.

published proceedings

  • Biochim Biophys Acta

author list (cited authors)

  • Berg, R. A., Kishida, Y., Kobayashi, Y., Inouye, K., Tonelli, A. E., Sakakibara, S., & Prockop, D. J.

citation count

  • 37

complete list of authors

  • Berg, RA||Kishida, Y||Kobayashi, Y||Inouye, K||Tonelli, AE||Sakakibara, S||Prockop, DJ

publication date

  • January 1973