Description: Hemoglobin Dynamics in Red Blood Cells: Correlation to Body Temperature

This title appears in the Scientific Report : 2008

Hemoglobin Dynamics in Red Blood Cells: Correlation to Body Temperature

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 temperatur...

Personal Name(s):	Stadler, A.M.
	Digel, I. / Artmann, G.M. / Embs, J.P. / Zaccai, G. / Büldt, G.
Contributing Institute:	Molekulare Biophysik; INB-2
Published in:	Biophysical journal, 95 (2008) S. 5449 - 5461
Imprint:	New York, NY Rockefeller Univ. Press 2008
Physical Description:	5449 - 5461
DOI:	10.1529/biophysj.108.138040
PubMed ID:	18708462
Document Type:	Journal Article
Research Program:	Funktion und Dysfunktion des Nervensystems
Series Title:	Biophysical Journal 95
Subject (ZB):	Body Temperature Diffusion Elasticity Erythrocytes: metabolism Hemoglobins: metabolism Humans Neutron Diffraction Protein Denaturation Hemoglobins J
	Publikationsportal JuSER

Please use the identifier: http://dx.doi.org/10.1529/biophysj.108.138040 in citations.

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.