001     508
005     20240619083250.0
024 7 _ |2 pmid
|a pmid:19044852
024 7 _ |2 DOI
|a 10.1063/1.2951987
024 7 _ |2 WOS
|a WOS:000259008900044
024 7 _ |2 Handle
|a 2128/4643
037 _ _ |a PreJuSER-508
041 _ _ |a eng
082 _ _ |a 540
084 _ _ |2 WoS
|a Physics, Atomic, Molecular & Chemical
100 1 _ |0 P:(DE-Juel1)VDB71338
|a Gögelein, C.
|b 0
|u FZJ
245 _ _ |a A simple patchy colloid model for the phase behavior of lysozyme dispersions
260 _ _ |a Melville, NY
|b American Institute of Physics
|c 2008
300 _ _ |a 085102
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 |0 3145
|a Journal of Chemical Physics
|v 129
|x 0021-9606
500 _ _ |a This project has been partly supported by the European Commission under the 6th Framework Program through integrating and strengthening the European Research Area. Contract No. SoftComp, NoE/NMP3-CT-2004-502235.
520 _ _ |a We propose a minimal model for spherical proteins with aeolotopic pair interactions to describe the equilibrium phase behavior of lysozyme. The repulsive screened Coulomb interactions between the particles are taken into account assuming that the net charges are smeared out homogeneously over the spherical protein surfaces. We incorporate attractive surface patches, with the interactions between patches on different spheres modeled by an attractive Yukawa potential. The parameters entering the attractive Yukawa potential part are determined using information on the experimentally accessed gas-liquid-like critical point. The Helmholtz free energy of the fluid and solid phases is calculated using second-order thermodynamic perturbation theory. Our predictions for the solubility curve are in fair agreement with experimental data. In addition, we present new experimental data for the gas-liquid coexistence curves at various salt concentrations and compare these with our model calculations. In agreement with earlier findings, we observe that the strength and the range of the attractive potential part only weakly depend on the salt content.
536 _ _ |0 G:(DE-Juel1)FUEK414
|2 G:(DE-HGF)
|a Kondensierte Materie
|c P54
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Algorithms
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Biophysics: methods
650 _ 2 |2 MeSH
|a Chemistry, Physical: methods
650 _ 2 |2 MeSH
|a Chickens
650 _ 2 |2 MeSH
|a Colloids: chemistry
650 _ 2 |2 MeSH
|a Egg Proteins: chemistry
650 _ 2 |2 MeSH
|a Hydrogen-Ion Concentration
650 _ 2 |2 MeSH
|a Models, Statistical
650 _ 2 |2 MeSH
|a Models, Theoretical
650 _ 2 |2 MeSH
|a Muramidase: chemistry
650 _ 2 |2 MeSH
|a Solubility
650 _ 2 |2 MeSH
|a Solvents: chemistry
650 _ 2 |2 MeSH
|a Temperature
650 _ 2 |2 MeSH
|a Thermodynamics
650 _ 7 |0 0
|2 NLM Chemicals
|a Colloids
650 _ 7 |0 0
|2 NLM Chemicals
|a Egg Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Solvents
650 _ 7 |0 EC 3.2.1.17
|2 NLM Chemicals
|a Muramidase
650 _ 7 |2 WoSType
|a J
700 1 _ |0 P:(DE-Juel1)130858
|a Nägele, G.
|b 1
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB10252
|a Tuinier, R.
|b 2
|u FZJ
700 1 _ |0 P:(DE-HGF)0
|a Gibaud, T.
|b 3
700 1 _ |0 P:(DE-HGF)0
|a Stradner, A.
|b 4
700 1 _ |0 P:(DE-HGF)0
|a Schurtenberger, P.
|b 5
773 _ _ |0 PERI:(DE-600)1473050-9
|a 10.1063/1.2951987
|g Vol. 129, p. 085102
|p 085102
|q 129<085102
|t The @journal of chemical physics
|v 129
|x 0021-9606
|y 2008
856 7 _ |u http://dx.doi.org/10.1063/1.2951987
856 4 _ |u https://juser.fz-juelich.de/record/508/files/4643.pdf
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920 1 _ |0 I:(DE-Juel1)VDB787
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