Hauptseite > Publikationsdatenbank > Viscosity and diffusion: crowding and salt effects in protein solutions > print

001     17773
005     20240619083339.0
024 7 _ |2 DOI
|a 10.1039/c1sm06242e
024 7 _ |2 WOS
|a WOS:000298990600019
024 7 _ |a 2128/4632
|2 Handle
037 _ _ |a PreJuSER-17773
082 _ _ |a 530
100 1 _ |a Heinen, M.
|b 0
|u FZJ
|0 P:(DE-Juel1)VDB86654
245 _ _ |a Viscosity and diffusion: crowding and salt effects in protein solutions
260 _ _ |a Cambridge
|b Royal Society of Chemistry (RSC)
|c 2012
300 _ _ |a 1404-1419
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Soft Matter
|x 1744-683X
|0 16881
|y 0
|v 0
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a We report on a joint experimental–theoretical study of collective diffusion in, and static shear viscosity of solutions of bovine serum albumin (BSA) proteins, focusing on the dependence on protein and salt concentration. Data obtained from dynamic light scattering and rheometric measurements are compared to theoretical calculations based on an analytically treatable spheroid model of BSA with isotropic screened Coulomb plus hard-sphere interactions. The only input to the dynamics calculations is the static structure factor obtained from a consistent theoretical fit to a concentration series of small-angle X-ray scattering (SAXS) data. This fit is based on an integral equation scheme that combines high accuracy with low computational cost. All experimentally probed dynamic and static properties are reproduced theoretically with an at least semi-quantitative accuracy. For lower protein concentration and low salinity, both theory and experiment show a maximum in the reduced viscosity, caused by the electrostatic repulsion of proteins. On employing our theoretical and experimental results, the applicability range of a generalized Stokes–Einstein (GSE) relation connecting viscosity, collective diffusion coefficient, and osmotic compressibility, proposed by Kholodenko and Douglas [Phys. Rev. E, 1995, 51, 1081] is examined. Significant violation of the GSE relation is found, both in experimental data and in theoretical models, in concentrated systems at physiological salinity, and under low-salt conditions for arbitrary protein concentrations.
536 _ _ |a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
|c P45
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK505
|x 0
700 1 _ |a Zanini, F.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Roosen-Runge, F.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Fedunová, D.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Zhang, F.
|b 4
|0 P:(DE-HGF)0
700 1 _ |a Hennig, M.
|b 5
|0 P:(DE-HGF)0
700 1 _ |a Seydel, T.
|b 6
|0 P:(DE-HGF)0
700 1 _ |a Schweins, R.
|b 7
|0 P:(DE-HGF)0
700 1 _ |a Sztucki, M.
|b 8
|0 P:(DE-HGF)0
700 1 _ |a Antalik, M.
|b 9
|0 P:(DE-HGF)0
700 1 _ |a Schreiber, F.
|b 10
|0 P:(DE-HGF)0
700 1 _ |a Nägele, G.
|b 11
|u FZJ
|0 P:(DE-Juel1)130858
773 _ _ |a 10.1039/c1sm06242e
|g Vol. 8
|p 1404-1419
|0 PERI:(DE-600)2191476-X
|t Soft matter
|v 8
|y 2012
|x 1744-683X
|n 5
856 7 _ |u http://dx.doi.org/10.1039/c1sm06242e
856 4 _ |u https://juser.fz-juelich.de/record/17773/files/4632.pdf
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/17773/files/FZJ-17773.pdf
|y Published under German "Allianz" Licensing conditions on 2011-11-29. Available in OpenAccess from 2012-11-29
|z Published final document.
856 4 _ |u https://juser.fz-juelich.de/record/17773/files/4632.jpg?subformat=icon-1440
|x icon-1440
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/17773/files/4632.jpg?subformat=icon-180
|x icon-180
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/17773/files/4632.jpg?subformat=icon-640
|x icon-640
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/17773/files/FZJ-17773.jpg?subformat=icon-1440
|x icon-1440
856 4 _ |u https://juser.fz-juelich.de/record/17773/files/FZJ-17773.jpg?subformat=icon-180
|x icon-180
856 4 _ |u https://juser.fz-juelich.de/record/17773/files/FZJ-17773.jpg?subformat=icon-640
|x icon-640
909 C O |o oai:juser.fz-juelich.de:17773
|p openaire
|p open_access
|p driver
|p VDB
|p dnbdelivery
913 1 _ |k P45
|v BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
|l Biologische Informationsverarbeitung
|b Schlüsseltechnologien
|0 G:(DE-Juel1)FUEK505
|x 0
913 2 _ |a DE-HGF
|b Key Technologies
|l BioSoft Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences
|1 G:(DE-HGF)POF3-550
|0 G:(DE-HGF)POF3-551
|2 G:(DE-HGF)POF3-500
|v Functional Macromolecules and Complexes
|x 0
914 1 _ |y 2012
915 _ _ |a JCR/ISI refereed
|0 StatID:(DE-HGF)0010
|2 StatID
915 _ _ |a JCR
|0 StatID:(DE-HGF)0100
|2 StatID
915 _ _ |a WoS
|0 StatID:(DE-HGF)0110
|2 StatID
|b Science Citation Index
915 _ _ |a WoS
|0 StatID:(DE-HGF)0111
|2 StatID
|b Science Citation Index Expanded
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0150
|2 StatID
|b Web of Science Core Collection
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0199
|2 StatID
|b Thomson Reuters Master Journal List
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0200
|2 StatID
|b SCOPUS
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0300
|2 StatID
|b Medline
915 _ _ |a Allianz-Lizenz / DFG
|0 StatID:(DE-HGF)0400
|2 StatID
915 _ _ |a Nationallizenz
|0 StatID:(DE-HGF)0420
|2 StatID
915 _ _ |a OpenAccess
|0 StatID:(DE-HGF)0510
|2 StatID
915 _ _ |a Allianz-OA
|0 StatID:(DE-HGF)0520
|2 StatID
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)1020
|2 StatID
|b Current Contents - Social and Behavioral Sciences
920 1 _ |k ICS-3
|l Weiche Materie
|g ICS
|0 I:(DE-Juel1)ICS-3-20110106
|x 0
970 _ _ |a VDB:(DE-Juel1)132338
980 1 _ |a FullTexts
980 _ _ |a VDB
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)ICS-3-20110106
980 _ _ |a UNRESTRICTED
980 _ _ |a JUWEL
980 _ _ |a JUWEL
980 _ _ |a FullTexts

LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21