title: Fuzzy complexes of myelin basic protein: NMR spectroscopic investigations of a polymorphic organizational linker of the central nervous system.
abstract: The classic 18.5 kDa isoform of myelin basic protein (MBP) is central to maintaining the structural homeostasis of the myelin sheath of the central nervous system. It is an intrinsically disordered, promiscuous, multifunctional, peripheral membrane protein, whose conformation adapts to its particular environment. Its study requires the selective and complementary application of diverse approaches, of which solution and solid-state NMR spectroscopy are the most powerful to elucidate site-specific features. We review here several recent solution and solid-state NMR spectroscopic studies of 18.5 kDa MBP, and the induced partial disorder-to-order transitions that it has been demonstrated to undergo when complexed with calmodulin, actin, and phospholipid membranes.
authors.affiliation: Centre for Structural Biology, Institute of Fundamental Sciences, Department of Physics, Massey University, Palmerston North, New Zealand. d.s.libich@massey.ac.nz
authors.forename: David S
authors.initials: DS
authors.lastname: Libich
authors.forename: Mumdooh A M
authors.initials: MA
authors.lastname: Ahmed
authors.forename: Ligang
authors.initials: L
authors.lastname: Zhong
authors.forename: Vladimir V
authors.initials: VV
authors.lastname: Bamm
authors.forename: Vladimir
authors.initials: V
authors.lastname: Ladizhansky
authors.forename: George
authors.initials: G
authors.lastname: Harauz
mesh_terms: D000818:Animals; D002490:Central Nervous System / Q000737:chemistry*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D004676:Myelin Basic Protein / Q000737:chemistry*; D011487:Protein Conformation; D020033:Protein Isoforms / Q000737:chemistry*
chemical_list: D004676:Myelin Basic Protein; D020033:Protein Isoforms
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