ArticleEuropean biophysics journal : EBJ2009
Dynamics of apomyoglobin in the alpha-to-beta transition and of partially unfolded aggregated protein.
Article in European biophysics journal : EBJ, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Direct Evidence for the Effect of Glycerol on Protein Hydration and Thermal Structural Transition.Biophysical journal · 2018Article
- Complex kinetics and residual structure in the thermal unfolding of yeast triosephosphate isomerase.BMC biochemistry · 2015Article
- Correlation between supercoiling and conformational motions of the bacterial flagellar filament.Biophysical journal · 2013Article
- Misfolding and amyloid aggregation of apomyoglobin.International journal of molecular sciences · 2013Review
- Change of dynamics of raft-model membrane induced by amyloid-β protein binding.The European physical journal. E, Soft matter · 2013Article
- Neutron scattering: a tool to detect in vivo thermal stress effects at the molecular dynamics level in micro-organisms.Journal of the Royal Society, Interface · 2013Article
- Article
- Thermal fluctuations of haemoglobin from different species: adaptation to temperature via conformational dynamics.Journal of the Royal Society, Interface · 2012Article
- Dynamics-stability relationships in apo- and holomyoglobin: a combined neutron scattering and molecular dynamics simulations study.Biophysical journal · 2012Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
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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Registered trials
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