Dynamics of apomyoglobin in the α-to-β transition and of partially unfolded aggregated protein

Abstract

Changes of molecular dynamics in the α-to-β transition associated with amyloid fibril formation were explored on apomyoglobin (ApoMb) as a model system. Circular dichroism, neutron and X-ray scattering experiments were performed as a function of temperature on the protein, at different solvent conditions. A significant change in molecular dynamics was… (More)
DOI: 10.1007/s00249-008-0375-z

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