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.
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.
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
D004676:Myelin Basic Protein; D018996:Myelin P2 Protein; D010455:Peptides