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000018195 0247_ $$2DOI$$a10.1007/s00249-011-0678-3
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000018195 084__ $$2WoS$$aBiophysics
000018195 1001_ $$0P:(DE-Juel1)VDB103059$$aAppavou, M-S.$$b0$$uFZJ
000018195 245__ $$aThe influence of 2 kbar pressure on the global and internal dynamics of human hemoglobin observed by quasielastic neutron scattering
000018195 260__ $$aBerlin$$bSpringer$$c2011
000018195 29510 $$a..
000018195 300__ $$a705 - 714
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000018195 440_0 $$010441$$aEuropean Biophysics Journal : with Biophysics Letters$$v40$$x0175-7571$$y6
000018195 500__ $$aThe research project was supported by a grant of the Deutsche Forschungsgemeinschaft, SFB 533, TP B11, which is gratefully acknowledged. We would like to acknowledge particularly Joachim Dorbecker and Reinhold Funer who helped to build the 2 kbar pressure cell and the platform for TOFTOF. We would like to thank Jandal Ringe for his help on TOFTOF during our experiments. The ANTARES team, especially Martin Muhlbauer and Elbio Calzada, are thanked for allowing us to use some beam time for neutronography measurements, and to Robert Georgii for beamtime on MIRA to perform the SANS characterization measurements. Finally, we would like to thank Alan Soper for useful discussions.
000018195 520__ $$aPressure is a ubiquitous physical parameter in life and is commonly used in the life sciences to study new protein folding pathways or association-dissociation phenomena. In this paper, an investigation of the influence of pressure on hemoglobin, a multimeric protein, at the picosecond time scale is presented using time-of-flight neutron scattering. The aim is to observe the influence of pressure on the translational diffusion and internal motions of hemoglobin in a concentrated solution and a possible dissociation of the subunits as suggested by Pin et al. (Biochemistry 29:9194, 1990) using fluorescence spectroscopy. A new flat 2 kbar pressure cell made of an aluminum alloy has been used, which allowed the effect of pressure to be studied with minimum background contribution. Within this range of pressure, the effect of this physical parameter on global diffusion can be explained in terms of the change in the water buffer viscosity and an oligomerization of hemoglobin subunits, whereas the internal motions were less affected.
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000018195 65320 $$2Author$$aPressure
000018195 65320 $$2Author$$aProtein
000018195 65320 $$2Author$$aHemoglobin
000018195 65320 $$2Author$$aDynamics
000018195 65320 $$2Author$$aQuasielastic neutron scattering
000018195 650_2 $$2MeSH$$aDiffusion
000018195 650_2 $$2MeSH$$aHemoglobin Subunits: chemistry
000018195 650_2 $$2MeSH$$aHumans
000018195 650_2 $$2MeSH$$aMotion
000018195 650_2 $$2MeSH$$aNeutron Diffraction: methods
000018195 650_2 $$2MeSH$$aPressure
000018195 650_2 $$2MeSH$$aProtein Conformation
000018195 650_2 $$2MeSH$$aScattering, Radiation
000018195 650_2 $$2MeSH$$aViscosity
000018195 650_7 $$00$$2NLM Chemicals$$aHemoglobin Subunits
000018195 650_7 $$2WoSType$$aJ
000018195 65027 $$0V:(DE-MLZ)SciArea-160$$2V:(DE-HGF)$$aBiology$$x0
000018195 65017 $$0V:(DE-MLZ)GC-130-2016$$2V:(DE-HGF)$$aHealth and Life$$x1
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000018195 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
000018195 7001_ $$0P:(DE-HGF)0$$aBusch, S.$$b1
000018195 7001_ $$0P:(DE-HGF)0$$aDoster, W.$$b2
000018195 7001_ $$0P:(DE-HGF)0$$aGaspar, A.$$b3
000018195 7001_ $$0P:(DE-HGF)0$$aUnruh, T.$$b4
000018195 773__ $$0PERI:(DE-600)1398349-0$$a10.1007/s00249-011-0678-3$$gVol. 40, p. 705 - 714$$p705 - 714$$q40<705 - 714$$tEuropean biophysics journal$$v40$$x0175-7571$$y2011
000018195 8567_ $$uhttp://dx.doi.org/10.1007/s00249-011-0678-3
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