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000005171 0247_ $$2DOI$$a10.1021/ja807691j
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000005171 041__ $$aeng
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000005171 084__ $$2WoS$$aChemistry, Multidisciplinary
000005171 1001_ $$0P:(DE-Juel1)VDB78506$$aStadler, A.M.$$b0$$uFZJ
000005171 245__ $$aCytoplasmic Water and Hydration Layer Dynamics in Human Red Blood Cells
000005171 260__ $$aWashington, DC$$bAmerican Chemical Society$$c2008
000005171 300__ $$a16852 - 16853
000005171 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000005171 440_0 $$08502$$aJournal of the American Chemical Society$$v130$$x0002-7863$$y50
000005171 500__ $$aWe thank Franz Dernmel for help with the experiment on IRIS, Aysegul Temiz Artmann and Dariusz Porst for help during sample preparation, and Moeava Tehei and Marion Jasnin for fruitful discussions. This work is based on experiments performed at the neutron sources SINQ FRM II and ISIS. This research project has been supported by the European Commission under the sixth Framework Programme through the Key Action: Strengthening the European Research Area, Research Infrastructures. Contract No: RII3-CT-2003-505925.
000005171 520__ $$aThe dynamics of water in human red blood cells was measured with quasielastic incoherent neutron scattering in the temperature range between 290 and 320 K. Neutron spectrometers with time resolutions of 40, 13, and 7 ps were combined to cover time scales of bulk water dynamics to reduced mobility interfacial water motions. A major fraction of approximately 90% of cell water is characterized by a translational diffusion coefficient similar to bulk water. A minor fraction of approximately 10% of cellular water exhibits reduced dynamics. This slow water fraction was attributed to dynamically bound water on the surface of hemoglobin which accounts for approximately half of the hydration layer.
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000005171 650_2 $$2MeSH$$aCytoplasm: chemistry
000005171 650_2 $$2MeSH$$aErythrocytes: chemistry
000005171 650_2 $$2MeSH$$aHumans
000005171 650_2 $$2MeSH$$aWater: chemistry
000005171 650_7 $$07732-18-5$$2NLM Chemicals$$aWater
000005171 650_7 $$2WoSType$$aJ
000005171 693__ $$0EXP:(DE-MLZ)TOF-TOF-20140101$$1EXP:(DE-MLZ)FRMII-20140101$$5EXP:(DE-MLZ)TOF-TOF-20140101$$6EXP:(DE-MLZ)NL2au-20140101$$aForschungs-Neutronenquelle Heinz Maier-Leibnitz$$eTOFTOF: Cold neutron time-of-flight spectrometer$$fNL2au$$x0
000005171 7001_ $$0P:(DE-HGF)0$$aEmbs, J.P.$$b1
000005171 7001_ $$0P:(DE-HGF)0$$aDigel, I.$$b2
000005171 7001_ $$0P:(DE-HGF)0$$aArtmann, G.M.$$b3
000005171 7001_ $$0P:(DE-HGF)0$$aUnruh, T.$$b4
000005171 7001_ $$0P:(DE-Juel1)131957$$aBüldt, G.$$b5$$uFZJ
000005171 7001_ $$0P:(DE-HGF)0$$aZaccai, G.$$b6
000005171 773__ $$0PERI:(DE-600)1472210-0$$a10.1021/ja807691j$$gVol. 130, p. 16852 - 16853$$n50$$p16852 - 16853$$q130<16852 - 16853$$tJournal of the American Chemical Society$$v130$$x0002-7863$$y2008
000005171 8567_ $$uhttp://dx.doi.org/10.1021/ja807691j
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000005171 9201_ $$0I:(DE-Juel1)ISB-2-20090406$$d31.12.2010$$gISB$$kISB-2$$lMolekulare Biophysik$$x0
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