title: The secondary structure of myelin P2 protein derived by secondary structure prediction methods, circular dichroism, and 400-MHz 1H-NMR spectroscopy: implications for tertiary structure.
abstract: The various methods used to study the secondary and tertiary structure of myelin P2 protein, and one of its peptides (CN1), in aqueous solution, indicate that the native protein contains a significant fraction of alpha-helix, suggesting that the current prediction of an all-beta tertiary structure requires revision.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D004676:Myelin Basic Protein; D018996:Myelin P2 Protein; D010455:Peptides; D011487:Protein Conformation
chemical_list: D004676:Myelin Basic Protein; D018996:Myelin P2 Protein; D010455:Peptides