Fuzzy complexes of myelin basic protein: NMR spectroscopic investigations of a polymorphic organizational linker of the central nervous system

David S. Libich, Mumdooh A.M. Ahmed, Ligang Zhong, Vladimir V. Bamm, Vladimir Ladizhansky, George Harauz

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29 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)143-155
Number of pages13
JournalBiochemistry and Cell Biology
Issue number2
StatePublished - Apr 2010
Externally publishedYes



  • Actin
  • Calmodulin
  • Induced folding
  • Intrinsically disordered protein
  • Lipid bilayer
  • Membrane protein
  • Myelin basic protein
  • NMR spectroscopy

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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