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Updated: Jun 29, 2026

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
Published on: April 13, 2022
Dynamics of apomyoglobin in the alpha-to-beta transition and of partially unfolded aggregated protein
E Fabiani1, A M Stadler, D Madern
1Institut Laue-Langevin, BP156, Grenoble, France.
Abstract:
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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