D-h exchange during collagen-fold formation. Nucleation processest

A. Veis*, S. Ghosh, F. Jacobs

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

Nucleation of collagen-fold formation has been followed by D-H exchange techniques coupled with infra-red measurements of the Arnide II absorbance at 1550 cm-'. Solution Sephadex exchange and thin film exchange techniques were applied to two gelatin fractions differing in molecular weight and chain cross-linking. The exchange rate was measured at temperatures, T above and below the melting temperature, TM. At T> TM two classes of exchangeable H were detected. On the basis of their pD-rate profiles, these classes were assigned to pyrollidine ring rich chain sequences and t o the sequences deficient in these residues. At T< TM two additional classes were noted -a non-exchangeable group (the fold-nuclei) and a restricted exchange group probably adjacent to the fold-nuclei. It is proposed that nucleation begins in the pyrollidine residue rich regions but that there is a preliminary H-bonding in regions adjacent to the nuclei which must be reorganized before collagen-fold growth is propagated. Molecular weight and cross-linking are important in the growth rather than nucleation stages of renaturation.

Original languageEnglish (US)
Pages (from-to)135-143
Number of pages9
JournalConnective tissue research
Volume1
Issue number2
DOIs
StatePublished - Jan 1 1972

ASJC Scopus subject areas

  • Rheumatology
  • Biochemistry
  • Orthopedics and Sports Medicine
  • Molecular Biology
  • Cell Biology

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