Conformations of P2 Protein of Peripheral Nerve Myelin by Nuclear Magnetic Resonance Spectroscopy |
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| Authors: | B. E. Chapman G. E. James W. J. Moore |
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| Affiliation: | School of Chemistry, University of Sydney, New South Wales, Australia |
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| 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. |
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| Keywords: | Myelin P2 protein Nuclear magnetic resonance Protein-lipid interaction |
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