Comparison of Soluble and Native Elastin Conformations by Far-ultraviolet Circular Dichroism

Abstract

IN studying α-elastin¹, the soluble protein obtained from native elastin by acidic hydrolysis², we have found that the far-ultraviolet circular dichroism spectra in water and water–ethanol solutions give evidence for the presence of an α-helix conformation. This finding does not necessarily mean that the same conformation must also be present in the native insoluble protein, because of the chemical degradation used for its solubilization. On the other hand, the presence of some ordered structure in native elastin was suggested by X-ray diffraction patterns and other physical–chemical properties³, although no definite conclusion could be drawn on the actual molecular conformation.