ArticleBiophysical journal2009
From powder to solution: hydration dependence of human hemoglobin dynamics correlated to body temperature.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Impact of Sucrose as Osmolyte on Molecular Dynamics of Mouse Acetylcholinesterase.Biomolecules · 2020Article
- Article
- Temperature dependence of nanoscale dynamic processes measured in living millipedes by high resolution inelastic and elastic neutron scattering.Scientific reports · 2019Article
- Effect of Phosphorylation on a Human-like Osteopontin Peptide.Biophysical journal · 2017Article
- Dynamic footprint of sequestration in the molecular fluctuations of osteopontin.Journal of the Royal Society, Interface · 2015Article
- Correlation between supercoiling and conformational motions of the bacterial flagellar filament.Biophysical journal · 2013Article
- Perspectives in biological physics: the nDDB project for a neutron Dynamics Data Bank for biological macromolecules.The European physical journal. E, Soft matter · 2013Article
- Thermal fluctuations of haemoglobin from different species: adaptation to temperature via conformational dynamics.Journal of the Royal Society, Interface · 2012Article
- Dynamic properties of photosystem II membranes at physiological temperatures characterized by elastic incoherent neutron scattering. Increased flexibility associated with the inactivation of the oxygen evolving complex.Photosynthesis research · 2012Article
- Protein self-diffusion in crowded solutions.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Macromolecular dynamics in red blood cells investigated using neutron spectroscopy.Journal of the Royal Society, Interface · 2011Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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. 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 showed that amino acid side chains can explore larger volumes above body temperature than expected from normal temperature dependence. The body temperature transition in protein dynamics was absent in fully hydrated powder, indicating that picosecond protein dynamics responsible for the transition is activated only at a sufficient level of hydration. A collateral result from the study is that fully hydrated protein powder samples do not accurately describe all aspects of protein picosecond dynamics that might be necessary for biological function.
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