PMID: 6165808Jun 1, 1981Paper

Conformations of P2 protein of peripheral nerve myelin by nuclear magnetic resonance spectroscopy

Journal of Neurochemistry
B E ChapmanW J Moore

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.

References

Oct 1, 1977·Hoppe-Seyler's Zeitschrift für physiologische Chemie·W H ThomasK Hempel
Jul 1, 1977·Journal of Neurochemistry·K UyemuraK Kitamura
Jun 17, 1975·Proceedings of the Royal Society of London. Series B, Containing Papers of a Biological Character·I D CampbellJ P Williams
Dec 6, 1976·Biochemical and Biophysical Research Communications·B E Chapman, W J Moore
Nov 1, 1974·Journal of Neurochemistry·S W BrostoffH Wisniewski
Jun 1, 1970·Archives of Biochemistry and Biophysics·Y Oshiro, E H Eylar
May 1, 1980·Journal of Neurochemistry·G E James, W J Moore

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Citations

Aug 30, 1985·Chemistry and Physics of Lipids·J SundelinP A Peterson
Jul 1, 1987·Journal of the Neurological Sciences·P MilnerR A Hughes
Oct 6, 1998·Neuroreport·P RiccioP Cavatorta

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