The secondary structure of type i collagen N-telopeptide as demonstrated by Fourier transform IR spectroscopy and molecular modeling

Anne George*, James P. Malone, Arthur Veis

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

Abstract

The amino-telopeptides of type I collagen have been'implicated to have a crucial role in the events of fibril formation. The sequences have been highly conserved in a.variety of species. Several proposals have been presented to correlate the sequence.with structure and role in fibril formation, but no definite information on telopeptide structure has been deduced. The infrared spectrum of the amide I band, due almost entirely to the C=O stretch vibration'of peptide carbonyls, has been a most useful probe for determining the secondary structures of proteins in solution. In the . present sfudy, the secondary structure of a synthetic rat cl(I) amino-telopcptide has . been investigated in aqueous solution by Fourier transform infrared spectroscopy (FTIRS) using a 9-pass internal reflectance ZnSe prism cell. Conformational changes were monitored as the aqueous solution was'heated from 4 to 50°C by observing changes in the frequency position. The amide I band frequency shifted by about 10cm-1 when the aqueous telopeptide solution was heated from 4-50°C. Deconvolution of the amide I band showed that the major component could-be best represented as in a random configuration at 4°C but changed to a sheet with βturns around 30°C. To support these experimental data the telopeptide region was modeled using BIOSYM/MSI software on a Silicon Graphics R-4000, XIZ graphics workstation. The proposed telopeptide structure was energy minimized using DISCOVER CVFF repetitive build and minimize process to reduce steric hindrance and maximize Hbonding. The potential energy surface was quite low and the conformation was stabilized by only 3 H-bonds. This model suggests a telopeptide structure that can be induced to assume a conformation favorable for binding during its interchain interaction at the collagen helix cross-link (N-telopeptide) receptor domain around collagen residue 930.

Original languageEnglish (US)
Pages (from-to)121-131
Number of pages11
JournalProceedings of the Indian Academy of Sciences: Chemical Sciences
Volume111
Issue number1
StatePublished - 1999

Keywords

  • FTIR
  • Molecular modeling
  • Structure
  • Telopeptide

ASJC Scopus subject areas

  • Chemistry(all)

Fingerprint Dive into the research topics of 'The secondary structure of type i collagen N-telopeptide as demonstrated by Fourier transform IR spectroscopy and molecular modeling'. Together they form a unique fingerprint.

Cite this