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Mapping intramolecular distances of the 18.5-kDa Myelin Basic Protein under various conditions by Förster Resonance Energy Transfer

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Title: Mapping intramolecular distances of the 18.5-kDa Myelin Basic Protein under various conditions by Förster Resonance Energy Transfer
Author: Anonna, Prioti
Department: Department of Molecular and Cellular Biology
Program: Molecular and Cellular Biology
Advisor: George, Harauz
Abstract: The predominant 18.5-kDa isoform of Myelin Basic Protein (MBP) is essential for the development of myelin in the central nervous system (CNS), and is hyper-deiminated in multiple sclerosis. We have previously obtained intramolecular distances between several single Cys-substituted sites in unmodified and pseudo-deiminated MBP variants, and a single internal Trp residue, by Förster Resonance Energy Transfer (FRET). I have obtained additional constraints by FRET of fluorophores attached to double- and single-Cys-substituted residues in the presence of dodecylphosphocholine (DPC) and Zn2+ (to mimic the myelin membrane per se). The quenching of Trp fluorescence by the acceptor showed that Zn2+ in the presence of DPC at its critical micelle concentration of 1.25 mM affected MBP’s local tertiary fold, but FRET distances indicated a negligible effect on global structure. We showed that DPC, like trifluoroethanol (TFE), caused slight compaction and extension. No significant differences between the two variants were seen.
URI: http://hdl.handle.net/10214/17690
Date: 2019-12-13
Rights: Attribution-NonCommercial-NoDerivatives 4.0 International
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Attribution-NonCommercial-NoDerivatives 4.0 International Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivatives 4.0 International