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Circular dichroism spectra show abundance of β‐sheet structure in connectin, a muscle elastic protein
Author(s) -
Maruyama Koscak,
Itoh Yoshiharu,
Arisaka Fumio
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80717-7
Subject(s) - circular dichroism , random coil , titin , chemistry , protein secondary structure , crystallography , skeletal muscle , biophysics , anatomy , biochemistry , biology , myocyte , sarcomere , endocrinology
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].