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000000763 0247_ $$2DOI$$a10.1529/biophysj.108.138040
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000000763 084__ $$2WoS$$aBiophysics
000000763 1001_ $$0P:(DE-Juel1)VDB78506$$aStadler, A.M.$$b0$$uFZJ
000000763 245__ $$aHemoglobin Dynamics in Red Blood Cells: Correlation to Body Temperature
000000763 260__ $$aNew York, NY$$bRockefeller Univ. Press$$c2008
000000763 300__ $$a5449 - 5461
000000763 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000000763 440_0 $$0882$$aBiophysical Journal$$v95$$x0006-3495$$y11
000000763 500__ $$aThis 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.
000000763 520__ $$aA transition in hemoglobin behavior at close to body temperature has been discovered recently by micropipette aspiration experiments on single red blood cells (RBCs) and circular dichroism spectroscopy on hemoglobin solutions. The transition temperature was directly correlated to the body temperatures of a variety of species. In an exploration of the molecular basis for the transition, we present neutron scattering measurements of the temperature dependence of hemoglobin dynamics in whole human RBCs in vivo. The data reveal a change in the geometry of internal protein motions at 36.9 degrees C, at human body temperature. Above that temperature, amino acid side-chain motions occupy larger volumes than expected from normal temperature dependence, indicating partial unfolding of the protein. Global protein diffusion in RBCs was also measured and the findings compared favorably with theoretical predictions for short-time self-diffusion of noncharged hard-sphere colloids. The results demonstrated that changes in molecular dynamics in the picosecond time range and angstrom length scale might well be connected to a macroscopic effect on whole RBCs that occurs at body temperature.
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000000763 650_2 $$2MeSH$$aBody Temperature
000000763 650_2 $$2MeSH$$aDiffusion
000000763 650_2 $$2MeSH$$aElasticity
000000763 650_2 $$2MeSH$$aErythrocytes: metabolism
000000763 650_2 $$2MeSH$$aHemoglobins: metabolism
000000763 650_2 $$2MeSH$$aHumans
000000763 650_2 $$2MeSH$$aNeutron Diffraction
000000763 650_2 $$2MeSH$$aProtein Denaturation
000000763 650_7 $$00$$2NLM Chemicals$$aHemoglobins
000000763 650_7 $$2WoSType$$aJ
000000763 7001_ $$0P:(DE-HGF)0$$aDigel, I.$$b1
000000763 7001_ $$0P:(DE-HGF)0$$aArtmann, G.M.$$b2
000000763 7001_ $$0P:(DE-HGF)0$$aEmbs, J.P.$$b3
000000763 7001_ $$0P:(DE-HGF)0$$aZaccai, G.$$b4
000000763 7001_ $$0P:(DE-Juel1)131957$$aBüldt, G.$$b5$$uFZJ
000000763 773__ $$0PERI:(DE-600)1477214-0$$a10.1529/biophysj.108.138040$$gVol. 95, p. 5449 - 5461$$p5449 - 5461$$q95<5449 - 5461$$tBiophysical journal$$v95$$x0006-3495$$y2008
000000763 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2586580
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