Conformations of P2 protein of peripheral nerve myelin by nuclear magnetic resonance spectroscopy.
High-resolution 1H NMR spectra of P2 protein from bovine peripheral nerve myelin indicate that the protein contains a high degree of tertiary structure in aqueous solution. Denaturation of the protein in urea solutions is a multi-step process. Binding of lysophosphatidylcholine micelles to the protein causes a conformational change and a broadening of NMR peaks from side chains of aromatic amino acid and methionine residues, with much less effect on upfield methyl resonances.
D000818:Animals; D002417:Cattle; D005727:Ganglia, Spinal / Q000032:analysis; D008244:Lysophosphatidylcholines / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D004676:Myelin Basic Protein / Q000032:analysis*; D018996:Myelin P2 Protein; D011487:Protein Conformation / Q000187:drug effects; D011489:Protein Denaturation
D008244:Lysophosphatidylcholines; D004676:Myelin Basic Protein; D018996:Myelin P2 Protein