PMID: 7543406Jan 1, 1995Paper

Interactions of myelin basic protein with palmitoyllysophosphatidylcholine: characterization of the complexes and conformations of the protein

European Biophysics Journal : EBJ
G L MendzG B Ralston

Abstract

The stoichiometry of palmitoyllysophosphatidylcholine/myelin basic protein (PLPC/MBP) complexes, the location of the protein in the lysolipid micelles, and the conformational changes occurring in the basic protein and peptides derived from it upon interaction with lysolecithin micelles were investigated by circular dichroic spectropolarimetry, ultracentrifugation, electron paramagnetic resonance (EPR) and 31P, 13C, and 1H nuclear magnetic resonance spectroscopy (NMR), and electron magnetic resonance spectroscopy (NMR), and electron microscopy. Ultracentrifugation measurements indicated that well-defined complexes were formed by the association of one protein molecule with approximately 141 lysolipid molecules. Small-angle X-ray scattering data indicated that the PLPC/MBP complexes form particles with a radius of gyration of 3.8 nm. EPR spectral parameters of the spin labels 5-, and 16-doxylstearate incorporated into lysolecithin/basic protein aggregates, and 13C- and 1H-NMR relaxation times of PLPC indicated that the addition of the protein did not affect the environment and location of the labels and the organization of the lysolipid micelles. The data suggested that MBP lies primarily near the surface of the micelles, with se...Continue Reading

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Citations

Jun 29, 2004·Micron : the International Research and Review Journal for Microscopy·George HarauzChristophe Farès
Oct 26, 2000·Protein Expression and Purification·I R BatesG Harauz
Sep 18, 2002·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·David S Libich, George Harauz
Dec 16, 1998·Journal of Colloid and Interface Science·A A RivasR M Castro

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