Circular dichroism spectra show abundance of β‐sheet structure in connectin, a muscle elastic protein

Abstract Circular dichroism spectra of native connectin from chicken breast muscle strongly suggested the abundant presence of β-sheet structure, as much as 70% in 0.5 M KCl and 50 mM phosphate buffer, pH 7.5. α-Helix was not detected. These results are in contradiction with the conclusion that native connectin from rabbit skeletal muscle consists entirely of random coil [(1984) J. Mol. Biol. 180, 331-356].