Molecular dynamics exposes alpha-helices in myelin basic protein.

Ian R Bates; George Harauz

doi:10.1007/s00894-003-0145-x

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Molecular dynamics exposes alpha-helices in myelin basic protein.

Ian R Bates·George Harauz

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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.

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Animals Cell Membrane Computational Biology Humans Mice Models, Molecular Myelin Basic Protein Protein Structure, Secondary Protein Structure, Tertiary Journal Article Research Support, Non-U.S. Gov't

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Ian R Bates, George Harauz. 2003-07-24. Molecular dynamics exposes alpha-helices in myelin basic protein.. https://doi.org/10.1007/s00894-003-0145-x

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