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000004704 0247_ $$2DOI$$a10.1016/j.bpj.2009.03.043
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000004704 0247_ $$2MLZ$$aStadler2009
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000004704 041__ $$aeng
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000004704 084__ $$2WoS$$aBiophysics
000004704 1001_ $$0P:(DE-Juel1)VDB78506$$aStadler, A.M.$$b0$$uFZJ
000004704 245__ $$aFrom Powder to Solution: Hemoglobin Dynamics Correlated to Body Temperature
000004704 260__ $$aNew York, NY$$bRockefeller Univ. Press$$c2009
000004704 300__ $$a5073 - 5081
000004704 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000004704 440_0 $$0882$$aBiophysical Journal$$v96$$x0006-3495$$y12
000004704 500__ $$aThis work was supported by the European Commission under the 6th Framework Programme through the Key Action: Strengthening the European Research Area, Research Infrastructures (RII3-CT-2003-505925), the Institut Laue-Langevin (M.T.), and the AINSE (M.T.).
000004704 520__ $$aA transition in hemoglobin (Hb), involving partial unfolding and aggregation, has been shown previously by various biophysical methods. The correlation between the transition temperature and body temperature for Hb from different species, suggested that it might be significant for biological function. To focus on such biologically relevant human Hb dynamics, we studied the protein internal picosecond motions as a response to hydration, by elastic and quasielastic neutron scattering. Rates of fast diffusive motions were found to be significantly enhanced with increasing hydration from fully hydrated powder to concentrated Hb solution. In concentrated protein solution, the data showed that amino acid side chains can explore larger volumes above body temperature than expected from normal temperature dependence. The body temperature transition in protein dynamics was absent in fully hydrated powder, indicating that picosecond protein dynamics responsible for the transition is activated only at a sufficient level of hydration. A collateral result from the study is that fully hydrated protein powder samples do not accurately describe all aspects of protein picosecond dynamics that might be necessary for biological function.
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000004704 650_2 $$2MeSH$$aBody Temperature
000004704 650_2 $$2MeSH$$aElasticity
000004704 650_2 $$2MeSH$$aHemoglobins: chemistry
000004704 650_2 $$2MeSH$$aHumans
000004704 650_2 $$2MeSH$$aNeutrons
000004704 650_2 $$2MeSH$$aPowders
000004704 650_2 $$2MeSH$$aSolutions
000004704 650_2 $$2MeSH$$aWater: chemistry
000004704 650_7 $$00$$2NLM Chemicals$$aHemoglobins
000004704 650_7 $$00$$2NLM Chemicals$$aPowders
000004704 650_7 $$00$$2NLM Chemicals$$aSolutions
000004704 650_7 $$07732-18-5$$2NLM Chemicals$$aWater
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000004704 7001_ $$0P:(DE-HGF)0$$aDigel, I.$$b1
000004704 7001_ $$0P:(DE-HGF)0$$aEmbs, J.P.$$b2
000004704 7001_ $$0P:(DE-HGF)0$$aUnruh, T.$$b3
000004704 7001_ $$0P:(DE-HGF)0$$aZaccai, G.$$b4
000004704 7001_ $$0P:(DE-Juel1)131957$$aBüldt, G.$$b5$$uFZJ
000004704 7001_ $$0P:(DE-HGF)0$$aArtmann, G.$$b6
000004704 773__ $$0PERI:(DE-600)1477214-0$$a10.1016/j.bpj.2009.03.043$$gVol. 96, p. 5073 - 5081$$p5073 - 5081$$q96<5073 - 5081$$tBiophysical journal$$v96$$x0006-3495$$y2009
000004704 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2712052
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