Conformations of P2 Protein of Peripheral Nerve Myelin by Nuclear Magnetic Resonance Spectroscopy
- 1 June 1981
- journal article
- research article
- Published by Wiley in Journal of Neurochemistry
- Vol. 36 (6) , 2032-2036
- https://doi.org/10.1111/j.1471-4159.1981.tb10830.x
Abstract
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.Keywords
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