Structural transition temperature of hemoglobins correlates with species’ body temperature
- 28 March 2007
- journal article
- research article
- Published by Springer Science and Business Media LLC in European Biophysics Journal
- Vol. 37 (1), 1-10
- https://doi.org/10.1007/s00249-007-0144-4
Abstract
Human red blood cells (RBCs) exhibit sudden changes in their biophysical properties at body temperature (T B). RBCs were seen to undergo a spontaneous transition from blockage to passage at T C = 36.4 ± 0.3°C, when the temperature dependency of RBC-passages through 1.3 μm narrow micropipettes was observed. Moreover, concentrated hemoglobin solutions (45 g/dl) showed a viscosity breakdown between 36 and 37°C. With human hemoglobin, a structural transition was observed at T B as circular dichroism (CD) experiments revealed. This leads to the assumption that a species’ body temperature occupies a unique position on the temperature scale and may even be imprinted in the structure of certain proteins. In this study, it was investigated whether hemoglobins of species with a T B different from those of human show temperature transitions and whether those were also linked to the species’ T B. The main conclusion was drawn from dynamic light scattering (DLS) and CD experiments. It was observed that such structural temperature transitions did occur in hemoglobins from all studied species and were correlated linearly (slope 0.81, r = 0.95) with the species’ body temperature. We presumed that α-helices of hemoglobin were able to unfold more readily around T B. α-helical unfolding would initiate molecular aggregation causing RBC passage and viscosity breakdown as mentioned above. Thus, structural molecular changes of hemoglobin could determine biophysical effects visible on a macroscopic scale. It is hypothesized that the species’ body temperature was imprinted into the structure of hemoglobins.Keywords
This publication has 26 references indexed in Scilit:
- Body Temperature-Related Structural Transitions of Monotremal and Human HemoglobinBiophysical Journal, 2006
- 1.25 Å Resolution Crystal Structures of Human Haemoglobin in the Oxy, Deoxy and Carbonmonoxy FormsJournal of Molecular Biology, 2006
- Circular dichroism spectra of human hemoglobin reveal a reversible structural transition at body temperatureEuropean Biophysics Journal, 2004
- Myoglobin in crowded solutions: structure and diffusionChemical Physics, 2003
- Static and dynamic light scattering approach to the hydration of hemoglobin and its supertetramers in the presence of osmolitesPeptide Science, 2001
- CLUSTAL V: improved software for multiple sequence alignmentBioinformatics, 1992
- Translational diffusion of hemoglobin in human erythrocytes and hemolysatesJournal of Magnetic Resonance (1969), 1991
- Dynamical transition of myoglobin revealed by inelastic neutron scatteringNature, 1989
- Water of hydration in the intra- and extra-cellular environment of human erythrocytesBiochemistry and Cell Biology, 1988
- SANS studies of interacting hemoglobin in intact erythrocytesBiophysical Journal, 1988