Abstract
Collagen was labelled through tissue culture with [3,3,3-d3]alanine. 2HNMR spectra were obtained of the labelled collagen as fibrils and in solution using the quadrupolar echo technique for solids. The 2HNMR data were analysed in terms of a model for reorientation in which the molecule is considered to jump between two orientations in a time which is short compared to the residence time in each site, and short compared to (Δvq)−1. The best fit of the data indicates that the collagen molecule in the fibrils experiences reorientation about its long axis over an angular range of ∼30–40°. The T2 for [3,3,3-d3]alanine-labelled collagen fibrils is estimated to be ∼110 μS.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on SpringerLink
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Traub, W. & Piez, K. A. Adv. Protein Chem. 25, 243–352 (1971).
Piez, K. A. in Biochemistry of Collagen (eds Ramachandran, G. N. & Reddi, A. H.) 1–44 (Plenum, New York, 1976).
Ramachandran, G. N. & Ramakrishnan, C. in Biochemistry of Collagen (eds Ramachandran, G. N. & Reddi, A. H.) 45–84 (Plenum, New York, 1976).
Ramachandran, G. N. in Treatise on Collagen (ed. Ramachandran, G. N.) 102–183 (Academic, New York, 1967).
Jelinski, L. W. & Torchia, D. A. J. molec. Biol. 133, 45–65 (1979).
Jelinski, L. W. & Torchia, D. A. J. molec. Biol. (in the press).
Mantsch, H. H., Saito, H. & Smith, I. C. P. Prog. nuclear magn. Resonance Spectrosc. 11, 211–272 (1977).
Slichter, C. P. Principles of Magnetic Resonance 62–76 (Springer, New York, 1978).
Siegel, R. C. & Fu, J. C. C. J. biol. Chem. 251, 5779–5785 (1976).
Piez, K. A. & Carrillo, A. L. Biochemistry 3, 908–914 (1964).
Hill, J. & Leach, S. J. Biochemistry 3, 1814–1818 (1964).
Davis, J. H., Jeffrey, K. R., Bloom, M., Valic, M. I. & Higgs, T. P. Chem. phys. Lett. 42, 390–394 (1976).
Blinc, R., Rutar, V., Seliger, J., Slak, J. & Smolej, V. Chem phys. Lett. 48, 576–578 (1977).
Hentschel, R. & Spiess, H. W. J. Magn. Resonance 35, 157–162 (1979).
Burnett, L. J. & Muller, B. H. J. chem. Phys. 55, 5829–5831 (1971).
Rice, D. & Oldfield, E. Biochemistry 18, 3272–3279 (1979).
Thomas, J. C. & Fletcher, G. C. Biopolymers 18, 1333–1352 (1979).
Fraser, R. D. B., MacRae, T. P. & Suzuki, E. J. molec. Biol. 129, 463–481 (1979).
Mehring, M. in NMR—Basic Principles and Progress, Vol. 11 (eds Diehl, P., Fluck, E. & Kosfeld, R.) 30–39 (Springer, New York, 1976).
Torchia, D. A. & VanderHart, D. L. J. molec. Biol. 104, 315–321 (1976).
Lehmann, M. S., Koetzle, T. F. & Hamilton, W. C. J. Am. chem. Soc. 94, 2657–2660 (1972).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Jelinski, L., Sullivan, C. & Torchia, D. 2H NMR study of molecular motion in collagen fibrils. Nature 284, 531–534 (1980). https://doi.org/10.1038/284531a0
Received:
Accepted:
Issue date:
DOI: https://doi.org/10.1038/284531a0
This article is cited by
-
Determination of methyl order parameters using solid state NMR under off magic angle spinning
Journal of Biomolecular NMR (2019)
-
Proline provides site-specific flexibility for in vivo collagen
Scientific Reports (2018)
-
Effects of amantadine on the dynamics of membrane-bound influenza A M2 transmembrane peptide studied by NMR relaxation
Journal of Biomolecular NMR (2009)
-
Quantitative Monitoring of Extracellular Matrix Production in Bone Implants by 13C and 31P Solid-State Nuclear Magnetic Resonance Spectroscopy
Calcified Tissue International (2007)
-
Dynamics of the biopolymers in articular cartilage studied by magic angle spinning NMR
Applied Magnetic Resonance (2004)
