title: Molecular dynamics exposes alpha-helices in myelin basic protein.
abstract: Molecular dynamics simulations of models of unmodified and deiminated MBP (myelin basic protein) have been performed on solvated structures with added counterions, for 10 ns using AMBER (assisted model building with energy refinement). The protein structures became extended, and a considerable number of alpha-helical segments formed spontaneously. The degree of molecular extension was greater in the deiminated species, and the alpha-helices were more transient. These structural disruptions may be operative in vivo during multiple sclerosis.
authors.affiliation: Department of Molecular Biology and Genetics, and Biophysics Interdepartmental Group, University of Guelph, 50 Stone Road East, N1G 2W1, Guelph, Ontario, Canada.
authors.forename: Ian R
authors.initials: IR
authors.lastname: Bates
authors.forename: George
authors.initials: G
authors.lastname: Harauz
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D019295:Computational Biology; D006801:Humans; D051379:Mice; D008958:Models, Molecular; D004676:Myelin Basic Protein / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D004676:Myelin Basic Protein