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- W650820457 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." @default.
- W650820457 created "2016-06-24" @default.
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- W650820457 creator A5085160326 @default.
- W650820457 date "2010-04-01" @default.
- W650820457 modified "2023-09-25" @default.
- W650820457 title "Fuzzy complexes of myelin basic protein: NMR spectroscopic investigations of a polymorphic organizational linker of the central nervous systemThis paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process." @default.
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- W650820457 doi "https://doi.org/10.1139/o09-123" @default.
- W650820457 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3517781" @default.
- W650820457 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20453917" @default.