Journal Article

PreJuSER-763

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Hemoglobin Dynamics in Red Blood Cells: Correlation to Body Temperature

Stadler, A. M.FZJ* ; Digel, I. ; Artmann, G. M. ; Embs, J. P. ; Zaccai, G. ; Büldt, G.FZJ*

2008
Rockefeller Univ. Press New York, NY

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Please use a persistent id in citations: doi:10.1529/biophysj.108.138040

Abstract: A transition in hemoglobin behavior at close to body temperature has been discovered recently by micropipette aspiration experiments on single red blood cells (RBCs) and circular dichroism spectroscopy on hemoglobin solutions. The transition temperature was directly correlated to the body temperatures of a variety of species. In an exploration of the molecular basis for the transition, we present neutron scattering measurements of the temperature dependence of hemoglobin dynamics in whole human RBCs in vivo. The data reveal a change in the geometry of internal protein motions at 36.9 degrees C, at human body temperature. Above that temperature, amino acid side-chain motions occupy larger volumes than expected from normal temperature dependence, indicating partial unfolding of the protein. Global protein diffusion in RBCs was also measured and the findings compared favorably with theoretical predictions for short-time self-diffusion of noncharged hard-sphere colloids. The results demonstrated that changes in molecular dynamics in the picosecond time range and angstrom length scale might well be connected to a macroscopic effect on whole RBCs that occurs at body temperature.

Keyword(s): Body Temperature (MeSH) ; Diffusion (MeSH) ; Elasticity (MeSH) ; Erythrocytes: metabolism (MeSH) ; Hemoglobins: metabolism (MeSH) ; Humans (MeSH) ; Neutron Diffraction (MeSH) ; Protein Denaturation (MeSH) ; Hemoglobins ; J

Note: This research project was supported by the European Commission under the 6th Framework Programme through Key Action: Strengthening the European Research Area, Research Infrastructures, contract No. RII3-CT-2003505925.

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Contributing Institute(s):

1. Molekulare Biophysik (INB-2)

Research Program(s):

1. Funktion und Dysfunktion des Nervensystems (P33)

Appears in the scientific report 2008

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