Antifreeze glycoprotein. Conformational model based on vacuum ultraviolet circular dichroism data.

Circular dichroism spectra (CD) of an active fraction of antifreeze glycoprotein (AFGP) and of a lower molecular weight fraction which is less active are found to be similar in the wavelength range 170-230 nm. The contribution of the disaccharide side chain chromophores to the CD spectra of the glycoprotein is estimated from spectra of model oligosaccharides having similar structures. Comparison of the CD spectra of the peptide portion of AFGP to those of established model polypeptides suggests a 3-fold left-handed helix of the collagen type as the most likely conformation of the peptide. In the proposed model, the disaccharide moieties attached to every third residue are in identical environments. Furthermore, proline residues which are found in the less active fraction can be accommodated in this helical structure, consistent with the observed similarity of the spectra of the two fractions.