Abstract
THE first suggestions of a correlation between the thermal shrinkage of collagen and its amino-acid composition were made by Takahashi and Tanaka1 and Gustavson2,3. They found that the shrinkage temperature (TS) increased with the amount of hydroxyproline, and interpreted this as being a result of the hydrogen-bonding capacity of the hydroxyl group of this imino-acid. Later work, in particular that of Piez and Gross4, has shown that TS correlates equally well with proline content and that the sum of these two imino-acids gives the best correlation. Other workers5,6 have shown that the melting point of tropocollagen molecules in dilute solution (TD) varies in the same way with proline plus hydroxyproline. Regression coefficients obtained by Piez and Gross4 for plots of TS versus proline plus hydroxyproline indicate that these residues contribute equally to the thermal stabilization of the molecule and the bulk material, that is, it seems that hydroxyproline is either not hydrogen-bonded or, if it is, its contribution is negligible. It is thought that the basis of this correlation is the steric hindrance to rotation of one imino-acid residue with respect to another imino-acid residue when they are in adjacent positions along a chain7,8. In addition, Leach9 has pointed out that for the collagens he examined (serine plus threonine) appears to decrease with increase in TS, while the sum of the hydroxyamino-acid (serine, tyrosine, threonine and hydroxyproline) remains approximately the same.
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 Springer Link
- 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
Takahashi, T., and Tanaka, T., Bull. Japan Soc. Sci. Fisheries, 19, 603 (1953).
Gustavson, K. H., Svensk Kem. Tidskr., 65, 70 (1953).
Gustavson, K. H., The Chemistry and Reactivity of Collagen, 225 (Academic Press, New York, 1956).
Piez, K. A., and Gross, J., J. Biol. Chem., 235, 995 (1960).
Burge, R. E., and Hynes, R. D., J. Mol. Biol., 1, 155 (1959).
Harrington, W. F., and von Hippel, P. H., Adv. Prot. Chem., 16, 1 (1961).
Harrington, W. F., Nature, 181, 997 (1959).
von Hippel, P. H., and Harrington, W. F., Biochim. Biophys. Acta, 36, 427 (1959).
Leach, A. A., Biochem. J., 67, 83 (1957).
Josse, J., and Harrington, W. F., J. Mol. Biol., 9, 269 (1964).
Fujimoto, D., and Adams, E., Biochem. Biophys. Res. Commun., 17, 437 (1964).
Watson, M. R., and Silvester, N. R., Biochem. J., 71, 578 (1959).
Maser, M. D., and Rice, R. V., Biochim. Biophys. Acta, 63, 255 (1962).
Watson, M. R., Biochem. J., 68, 416 (1958).
Williams, A. P., Biochem. J., 74, 304 (1960).
Rigby, B. J., Biochem. Biophys. Acta, 47, 534 (1961).
Rosenburg, H., and Ennor, A. H., Biochem. J., 79, 424 (1961).
Urnes, P., and Doty, P., Adv. Prot. Chem., 16, 447 (1961).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
RIGBY, B. Correlation between Serine and Thermal Stability of Collagen. Nature 214, 87–88 (1967). https://doi.org/10.1038/214087a0
Issue Date:
DOI: https://doi.org/10.1038/214087a0
This article is cited by
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.