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European Biophysics Journal

, Volume 37, Issue 1, pp 1–10 | Cite as

Structural transition temperature of hemoglobins correlates with species’ body temperature

  • Kay Frank Thorsten Zerlin
  • Nicole Kasischke
  • Ilya Digel
  • Christina Maggakis-Kelemen
  • Aysegül Temiz Artmann
  • Dariusz Porst
  • Peter Kayser
  • Peter Linder
  • Gerhard Michael ArtmannEmail author
Original Paper

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

Protein dynamics Hemoglobin Structural transition Denaturation 

Notes

Acknowledgments

This work was financed by a grant from the Ministry of Innovation, Science, Research and Technology of the State of North Rhine-Westphalia to G. M. Artmann and by the Centre of Competence in Bioengineering at Juelich, Germany. We thank Jeff Turnage, San Diego Zoological Society, San Diego, CA, USA, for supplying animal blood samples. We thank Prof. Shu Chien and Prof. Y. C. Fung, Whittaker Institute for Bioengineering (UCSD), San Diego, for interesting and helpful discussions. Finally, we thank our colleagues Prof. G. Büldt and PD Dr. Fitter, Research Centre Juelich, for their support in structural biology. We also thank Prof. G. Dikta, who gave us excellent advice on statistical methods for turning point determinations.

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Copyright information

© EBSA 2007

Authors and Affiliations

  • Kay Frank Thorsten Zerlin
    • 1
  • Nicole Kasischke
    • 1
  • Ilya Digel
    • 1
  • Christina Maggakis-Kelemen
    • 1
  • Aysegül Temiz Artmann
    • 1
  • Dariusz Porst
    • 1
  • Peter Kayser
    • 1
  • Peter Linder
    • 1
  • Gerhard Michael Artmann
    • 1
    Email author
  1. 1.Division JuelichUniversity of Applied Sciences AachenJuelichGermany

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