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000019773 084__ $$2WoS$$aChemistry, Physical
000019773 084__ $$2WoS$$aPhysics, Atomic, Molecular & Chemical
000019773 1001_ $$0P:(DE-HGF)0$$aZhang, F.$$b0
000019773 245__ $$aHydration and interactions in protein solutions containing concentrated electrolytes studied by small-angle scattering
000019773 260__ $$aCambridge$$bRSC Publ.$$c2012
000019773 300__ $$a2483 - 2493
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000019773 440_0 $$04916$$aPhysical Chemistry Chemical Physics$$v14$$x1463-9076$$y7
000019773 500__ $$aWe gratefully acknowledge financial support from Deutsche Forschungsgemeinschaft (DFG) and the beam time allocation from ESRF, ILL, JCNS and Helmholtz-Center Berlin (BENSC). The beam time on V4 at the Helmholtz Zentrum Berlin has been supported by the European Commission under the 6th Framework Program through the Key Action: Strengthening the European Research Area, Research Infrastructures. Contract No. RII3-CT-2003-505925 (NMI3).
000019773 520__ $$aDuring protein crystallization and purification, proteins are commonly found in concentrated salt solutions. The exact interplay of the hydration shell, the salt ions, and protein-protein interactions under these conditions is far from being understood on a fundamental level, despite the obvious practical relevance. We have studied a model globular protein (bovine serum albumin, BSA) in concentrated salt solutions by small-angle neutron scattering (SANS). The data are also compared to previous studies using SAXS. The SANS results for dilute protein solutions give an averaged volume of BSA of 91,700 Å(3), which is about 37% smaller than that determined by SAXS. The difference in volume corresponds to the contribution of a hydration shell with a hydration level of 0.30 g g(-1) protein. The forward intensity I(0) determined from Guinier analysis is used to determine the second virial coefficient, A(2), which describes the overall protein interactions in solution. It is found that A(2) follows the reverse order of the Hofmeister series, i.e. (NH(4))(2)SO(4) < Na(2)SO(4) < NaOAc < NaCl < NaNO(3) < NaSCN. The dimensionless second virial coefficient B(2), corrected for the particle volume and molecular weight, has been calculated using different approaches, and shows that B(2) with corrections for hydration and the non-spherical shape of the protein describes the interactions better than those determined from the bare protein. SANS data are further analyzed in the full q-range using liquid theoretical approaches, which gives results consistent with the A(2) analysis and the experimental structure factor.
000019773 536__ $$0G:(DE-Juel1)FUEK505$$2G:(DE-HGF)$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x0
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000019773 650_2 $$2MeSH$$aAnimals
000019773 650_2 $$2MeSH$$aCattle
000019773 650_2 $$2MeSH$$aElectrolytes: chemistry
000019773 650_2 $$2MeSH$$aNeutron Diffraction
000019773 650_2 $$2MeSH$$aOsmolar Concentration
000019773 650_2 $$2MeSH$$aProtein Interaction Mapping
000019773 650_2 $$2MeSH$$aSalts: chemistry
000019773 650_2 $$2MeSH$$aScattering, Small Angle
000019773 650_2 $$2MeSH$$aSerum Albumin, Bovine: chemistry
000019773 650_2 $$2MeSH$$aX-Ray Diffraction
000019773 650_7 $$00$$2NLM Chemicals$$aElectrolytes
000019773 650_7 $$00$$2NLM Chemicals$$aSalts
000019773 650_7 $$00$$2NLM Chemicals$$aSerum Albumin, Bovine
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000019773 7001_ $$0P:(DE-HGF)0$$aRoosen-Runge, F.$$b1
000019773 7001_ $$0P:(DE-HGF)0$$aSkoda, M.W.A.$$b2
000019773 7001_ $$0P:(DE-Juel1)VDB97040$$aJacobs, R.M.J.$$b3$$uFZJ
000019773 7001_ $$0P:(DE-HGF)0$$aWolf, M.$$b4
000019773 7001_ $$0P:(DE-HGF)0$$aCallow, P.$$b5
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000019773 7001_ $$0P:(DE-HGF)0$$aPrévost, S.$$b8
000019773 7001_ $$0P:(DE-HGF)0$$aSchreiber, F.$$b9
000019773 773__ $$0PERI:(DE-600)1476244-4$$a10.1039/c2cp23460b$$gVol. 14, p. 2483 - 2493$$p2483 - 2493$$q14<2483 - 2493$$tPhysical Chemistry Chemical Physics$$v14$$x1463-9076$$y2012
000019773 8567_ $$uhttp://dx.doi.org/10.1039/c2cp23460b
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