Main content

Conformational Transitions of 18.5-kilodaltons Myelin Basic Protein Studied by Fluorescence Spectroscopy and Forster Resonance Energy Transfer

Show simple item record

dc.contributor.advisor Harauz, George
dc.contributor.author Jenkins, Andrew
dc.date.accessioned 2015-05-04T17:53:17Z
dc.date.available 2015-05-04T17:53:17Z
dc.date.copyright 2015-04
dc.date.created 2015-04-24
dc.date.issued 2015-05-04
dc.identifier.uri http://hdl.handle.net/10214/8793
dc.description.abstract The intrinsically-disordered, 18.5-kiloDalton (kDa) isoform of myelin basic protein (MBP) is a peripheral membrane protein that is essential to proper myelin formation in the central nervous system. MBP multifunctionality arises from its high conformational plasticity and its ability to undergo reversible disorder-to-order transitions. One such transition is the disorder-to-α-helical conformational change which is induced upon MBP-membrane binding. We have investigated the disorder-to-α-helical transition of MBP-derived α-peptides as well as of the full-length 18.5-kDa protein. The data suggest that the disorder-to-α-helical transition of MBP follows a three-state model: disordered↔intermediate↔α-helical, with each of the identified equilibrium states likely representing a conformational ensemble. The disordered state is characterized by slight compaction, whereas the intermediate globally more compact. This study suggests that multifunctionality in MBP could arise from differences in the population of energetically distinct ensemble clusters in different conditions and also provides an example of an IDP that undergoes cooperative global conformation change. en_US
dc.language.iso en en_US
dc.rights Attribution 2.5 Canada *
dc.rights.uri http://creativecommons.org/licenses/by/2.5/ca/ *
dc.subject ANS en_US
dc.subject FRET en_US
dc.subject Myelin Basic Protein en_US
dc.subject a-helical en_US
dc.subject a-helix en_US
dc.subject alpha-helical en_US
dc.subject Anilinonaphthalene en_US
dc.subject Bamm en_US
dc.subject binding-induced folding en_US
dc.subject Central Nervous System en_US
dc.subject Circular Dichroism en_US
dc.subject CNS en_US
dc.subject Conformational transitions en_US
dc.subject deconvolution en_US
dc.subject deconvolve en_US
dc.subject deimination en_US
dc.subject demyelinate en_US
dc.subject demyelination en_US
dc.subject disorder to a helical en_US
dc.subject disorder to order en_US
dc.subject disordered conformation en_US
dc.subject Fluoescence en_US
dc.subject Fluorescence Anisotropy en_US
dc.subject Fluorescence Spectroscopy en_US
dc.subject Forster Resonance Energy Transfer en_US
dc.subject Harauz en_US
dc.subject IAEDANS en_US
dc.subject IDP en_US
dc.subject Intrinsically disordered en_US
dc.subject Intrinsically disordered protein en_US
dc.subject Jenkins en_US
dc.subject kilodaltons en_US
dc.subject long range intramolecular folding en_US
dc.subject MBP en_US
dc.subject MBP-UTC1 en_US
dc.subject MBP-UTC8 en_US
dc.subject membrane mimetic solvents en_US
dc.subject MS en_US
dc.subject Multiple Sclerosis en_US
dc.subject mutagenesis en_US
dc.subject myelin sheath en_US
dc.subject neurodegeneration en_US
dc.subject oligodendrocyte en_US
dc.subject PAD2 en_US
dc.subject peptidylarginine deiminase type 2 en_US
dc.subject post-translational modification en_US
dc.subject PTM en_US
dc.subject random coil en_US
dc.subject recombinant en_US
dc.subject recombinant MBP en_US
dc.subject remyelinate en_US
dc.subject TFE en_US
dc.subject thermodynamic ensembles en_US
dc.subject titration curves en_US
dc.subject trifluoroethanal en_US
dc.subject Vassall en_US
dc.title Conformational Transitions of 18.5-kilodaltons Myelin Basic Protein Studied by Fluorescence Spectroscopy and Forster Resonance Energy Transfer en_US
dc.type Thesis en_US
dc.degree.programme Molecular and Cellular Biology en_US
dc.degree.name Master of Science en_US
dc.degree.department Department of Molecular and Cellular Biology en_US
dc.rights.license All items in the Atrium are protected by copyright with all rights reserved unless otherwise indicated.


Files in this item

Files Size Format View Description
Jenkins_Andrew_201504_Msc.pdf 2.346Mb PDF View/Open Thesis

This item appears in the following Collection(s)

Show simple item record

Attribution 2.5 Canada Except where otherwise noted, this item's license is described as Attribution 2.5 Canada