Abstract
THE strong bands at 3 µ, 6 µ and 6.5 µ which dominate the absorption spectra of proteins in the fundamental region, and which have been observed as well in N-monosubstituted amides and in synthetic polypeptides, have been attributed to vibrations of the peptide links between the amino-acid residues forming the structural backbone of the protein molecule1. It has been established, however, that, in most proteins, side-chains carrying ionizable groups are joined to the polypeptide backbone, and that at the isoionic point the protein exists in the form of dipolar ions. Of the ionizable groups which have been identified, carboxyls occur in the greatest number and may be expected to contribute significantly to the absorption processes in the spectral region of interest.
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
Sutherland, G. B. B. M., “Adv. in Protein Chem.” 7, 291 (1952).
Gore, R. C., Barnes, R. B., and Petersen, E., Anal. Chem., 21, 382 (1949).
Edsall, J. T., J. Chem. Phys., 5, 508 (1937).
Ambrose, E. J., and Elliott, A., Proc. Roy. Soc., A, 208, 75 (1951).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
EHRLICH, G., SUTHERLAND, G. Contribution of Side-Chains to the Infra-Red Spectra of Proteins: the 6.5-µ Band. Nature 172, 671–672 (1953). https://doi.org/10.1038/172671b0
Issue Date:
DOI: https://doi.org/10.1038/172671b0
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.