Preliminary studies of the secondary structure in solution of two phosphoproteins of chicken bone matrix by circular dichroism and fourier transform-infrared spectroscopy.

The secondary structures of two phosphoproteins from chicken bone matrix of Mr approximately 15kDa and approximately 28kDa, rich in Asx, Glx, and Ser, and containing Ser(P) and Thr(P) residues, have been investigated in solution by Circular Dichroism (CD) and Fourier Transform-Infrared Spectroscopy (FT-IR). CD spectroscopy, which yields useful information on the backbone conformation of polypeptides and proteins, suggests a predominantly beta-sheet structure for the two phosphoproteins. The FT-IR spectra of the approximately 15kDa protein, which is sensitive to secondary structure and hence provides complimentary information to CD spectroscopy, are consistent with the results obtained by CD studies.