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Protein Expr Purif 25:330-341īenfatto M, Della LS, Qin Y, Li Q, Pan G, Wu Z, Morante S (2004) The role of Zn in the interplay among Langmuir–Blodgett multilayer and myelin basic protein: a quantitative analysis of XANES spectra. Protein Expr Purif 20:285-299īates IR, Libich DS, Wood DD, Moscarello MA, Harauz G (2002) An Arg/Lys– > Gln mutant of recombinant murine myelin basic protein as a mimic of the deiminated form implicated in multiple sclerosis. J Biol Chem 234:466–468īates IR, Matharu P, Ishiyama N, Rochon D, Wood DD, Polverini E, Moscarello MA, Viner NJ, Harauz G (2000) Characterization of a recombinant murine 18.5-kDa myelin basic protein. Biochim Biophys Acta 1767:1073–1101īartlett G (1959) Phosphorus assay in column chromatography. Biochem Biophys Res Commun 391:224–229īarth A (2007) Infrared spectroscopy of proteins. Protein Expr Purif 62:36–43īaran C, Smith GS, Bamm VV, Harauz G, Lee JS (2010) Divalent cations induce a compaction of intrinsically disordered myelin basic protein. Biochemistry 40:11828–11840īamm VV, Harauz G (2008) Expression and purification of the active variant of recombinant murine Golli-interacting protein (GIP)-characterization of its phosphatase activity and interaction with Golli-BG21. Biophys J 96:180–191īailey RW, Dunker AK, Brown CJ, Garner EC, Griswold MD (2001) Clusterin, a binding protein with a molten globule-like region. When MBP was reconstituted with myelin-mimetic membranes, attenuated total reflectance-Fourier transform infrared spectroscopy revealed that there was a rearrangement of secondary structure components upon addition of zinc that was subtly different for each variant, indicative of a synergistic protein–membrane–cation interaction.Īhmed MA, Bamm VV, Shi L, Steiner-Mosonyi M, Dawson JF, Brown L, Harauz G, Ladizhansky V (2009) Induced secondary structure and polymorphism in an intrinsically disordered structural linker of the CNS: solid-state NMR and FTIR spectroscopy of myelin basic protein bound to actin.
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Circular dichroism spectroscopy showed that there was minimal effect of zinc on the secondary structure on MBP in aqueous solution. Isothermal titration calorimetry showed the dissociation constant to be in the micromolar range for all variants. In this study, we investigate the effect of zinc on different variants of 18.5 kDa MBP, including new recombinant forms lacking hexahistidine tags which would interfere with the binding of the cation. Zinc is an important stabilizing component of myelin and its concentration is substantially higher than that of any other trace element in the brain. It contains a high proportion of polar and charged amino acids, and has an adaptive conformation depending on its environment and binding surfaces (membranes) or partners (other proteins or small ligands including divalent cations). Myelin basic protein (MBP) is an essential structural protein required for tight compaction of the myelin sheath of the central nervous system, and belongs to the family of intrinsically disordered proteins.