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Full-Text Articles in Life Sciences
From Powder To Solution: Hydration Dependence Of Human Hemoglobin Dynamics Correlated To Body Temperature, A. M. Stadler, I. Digel, J. P. Embs, T. Unruh, Moeava Tehei, G. Zaccai, G. Büldt, G. M. Artmann
From Powder To Solution: Hydration Dependence Of Human Hemoglobin Dynamics Correlated To Body Temperature, A. M. Stadler, I. Digel, J. P. Embs, T. Unruh, Moeava Tehei, G. Zaccai, G. Büldt, G. M. Artmann
Faculty of Science - Papers (Archive)
A transition in hemoglobin (Hb), involving partial unfolding and aggregation, has been shown previously by various biophysical methods. The correlation between the transition temperature and body temperature for Hb from different species, suggested that it might be significant for biological function. In order to focus on such biologically relevant human Hb dynamics, we studied the protein internal picosecond motions as a response to hydration, by elastic and quasielastic neutron scattering. Rates of fast diffusive motions were found to be significantly enhanced with increasing hydration from fully hydrated powder to concentrated Hb solution. In concentrated protein solution, the data revealed that …
Dynamics Of Apomyoglobin In The Α-To-Β Transition And Of Partially Unfolded Aggregated Protein, E. Fabiani, A. M. Stadler, D. Madern, M. M. Koza, M. Tehei, M. Hirai, G. Zaccai
Dynamics Of Apomyoglobin In The Α-To-Β Transition And Of Partially Unfolded Aggregated Protein, E. Fabiani, A. M. Stadler, D. Madern, M. M. Koza, M. Tehei, M. Hirai, G. Zaccai
Faculty of Science - Papers (Archive)
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 …