Publication Details

This article was originally published as Fabiani, E, Stadler, AM, Madern, D, Koza, MM, Tehei, M, Hirai, M and Zaccai, G, Dynamics of apomyoglobin in the alpha-to-beta transition and of partially unfolded aggregated protein, European Biophysics Journal, 38 237-244 (2009). Published online 14 October, 2008. Copyright Springer Verlag 2008. Original journal article available here.


Changes of molecular dynamics in the α-to-β transition associated with amyloid fibril formation were explored on apo-myoglobin (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 observed at the α-to-β transition at about 55 ˚C, indicating a more resilient high temperature β structure phase. A similar effect at approximately the same temperature was observed in holo-myoglobin, associated with partial unfolding and protein aggregation. A study in a wide temperature range between 20 K and 360 K revealed that a dynamical transition at about 200 K for motions in the 50 ps time scale exists also for a hydrated powder of heat-denatured aggregated ApoMb.



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