Dynamics of apomyoglobin in the alpha-to-beta transition and of partially unfolded aggregated protein

作者：Fabiani E; Stadler A M; Madern D; Koza M M; Tehei M; Hirai M; Zaccai G^*

来源：European Biophysics Journal, 2009, 38(2): 237-244.

DOI：10.1007/s00249-008-0375-z

• Amyloid former
• Protein dynamics
• Neutron
• Circular dichroism

Changes of molecular dynamics in the alpha-to-beta 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 observed at the alpha-to-beta transition at about 55A degrees C, indicating a more resilient high temperature beta 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 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.

• 出版日期2009-2