Open AccessDynamics of apomyoglobin in the α-to-β transition and of partially unfolded aggregated protein
Author(s) -
E. Fabiani,
Andreas Stadler,
Dominique Madern,
Michael Marek Koza,
Moeava Tehei,
Mitsuhiro Hirai,
G. Zaccaï
Publication year - 2008
Publication title -
european biophysics journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 80
eISSN - 1432-1017
pISSN - 0175-7571
DOI - 10.1007/s00249-008-0375-z
Subject(s) - myoglobin , molecular dynamics , chemistry , circular dichroism , crystallography , phase transition , dynamics (music) , protein dynamics , chemical physics , neutron scattering , atmospheric temperature range , protein folding , thermodynamics , scattering , computational chemistry , organic chemistry , biochemistry , physics , acoustics , optics
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 55 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.
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