ArticleEuropean biophysics journal : EBJ2004
Circular dichroism spectra of human hemoglobin reveal a reversible structural transition at body temperature.
Article in European biophysics journal : EBJ, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- The thermal and storage stability of bovine haemoglobin by ultraviolet-visible and circular dichroism spectroscopies.Journal of pharmaceutical analysis · 2016Article
- Thermal-induced force release in oxyhemoglobin.Scientific reports · 2015Article
- Effects of spermine NONOate and ATP on protein aggregation: light scattering evidences.BMC biophysics · 2013Article
- Thermal fluctuations of haemoglobin from different species: adaptation to temperature via conformational dynamics.Journal of the Royal Society, Interface · 2012Article
- Effects of spermine NONOate and ATP on the thermal stability of hemoglobin.BMC biophysics · 2012Article
- The effects of temperature and pH on secondary structure and antioxidant activity of Crocodylus siamensis hemoglobin.The protein journal · 2012Article
- Macromolecular dynamics in red blood cells investigated using neutron spectroscopy.Journal of the Royal Society, Interface · 2011Article
- From powder to solution: hydration dependence of human hemoglobin dynamics correlated to body temperature.Biophysical journal · 2009Article
- Hemoglobin senses body temperature.European biophysics journal : EBJ · 2009Article
- Hemoglobin dynamics in red blood cells: correlation to body temperature.Biophysical journal · 2008Article
- Molecular processes in biological thermosensation.Journal of biophysics (Hindawi Publishing Corporation : Online) · 2008Article
- Structural transition temperature of hemoglobins correlates with species' body temperature.European biophysics journal : EBJ · 2007Article
- Body temperature-related structural transitions of monotremal and human hemoglobin.Biophysical journal · 2006Article
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Authors and funding
7 authors.
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Abstract
Previously we have shown that human red blood cells (RBCs) undergo a sudden change from blocking to passing through a 1.3+/-0.2-microm micropipette when applying an aspiration pressure of 2.3 kPa at a critical transition temperature (Tc = 36.4+/-0.3 degrees C). Low-shear viscosity measurements suggested that changes in the molecular properties of hemoglobin might be responsible for this effect. To evaluate structural changes in hemoglobin at the critical temperature, we have used circular dichroism (CD) spectroscopy. The thermal denaturation curves of human hemoglobin A (HbA) and hemoglobin S (HbS) upon heating between 25 and 60 degrees C were non-linear and showed accelerated denaturation between 35 and 39 degrees C with a midpoint at 37.2+/-0.6 degrees C. The transition was reversible below 39 degrees C and independent of solution pH (pH 6.8-7.8). It was also independent of the oxygenation state of hemoglobin, since a sample that was extensively deoxygenated with N2 showed a similar transition by CD. These findings suggest that a structural change in hemoglobin may enable the cellular passage phenomenon as well as the temperature-dependent decrease in viscosity of RBC solutions.
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