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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00005626naa a2200481 4500
001oai:DiVA.org:mau-45819
003SwePub
008210915s2021 | |||||||||||000 ||eng|
009oai:lup.lub.lu.se:1624fe2f-7a90-4617-8a15-b19119a1e3ab
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:mau:diva-458192 URI
0247 a https://doi.org/10.1039/d1sm00418b2 DOI
0247 a https://lup.lub.lu.se/record/1624fe2f-7a90-4617-8a15-b19119a1e3ab2 URI
040 a (SwePub)maud (SwePub)lu
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Beck, Christianu Univ Tubingen, Inst Angew Phys, Morgenstelle 10, D-72076 Tubingen, Germany.;Inst Max von Laue Paul Langevin, 71 Ave Martyrs, F-38042 Grenoble, France.,Institut Laue Langevin,University of Tübingen4 aut
2451 0a Temperature and salt controlled tuning of protein clusters
264 c 2021
264 1b Royal Society of Chemistry,c 2021
338 a electronic2 rdacarrier
520 a The formation of molecular assemblies in protein solutions is of strong interest both from a fundamental viewpoint and for biomedical applications. While ordered and desired protein assemblies are indispensable for some biological functions, undesired protein condensation can induce serious diseases. As a common cofactor, the presence of salt ions is essential for some biological processes involving proteins, and in aqueous suspensions of proteins can also give rise to complex phase diagrams including homogeneous solutions, large aggregates, and dissolution regimes. Here, we systematically study the cluster formation approaching the phase separation in aqueous solutions of the globular protein BSA as a function of temperature (T), the protein concentration (c(p)) and the concentrations of the trivalent salts YCl3 and LaCl3 (c(s)). As an important complement to structural, i.e. time-averaged, techniques we employ a dynamical technique that can detect clusters even when they are transient on the order of a few nanoseconds. By employing incoherent neutron spectroscopy, we unambiguously determine the short-time self-diffusion of the protein clusters depending on c(p), c(s) and T. We determine the cluster size in terms of effective hydrodynamic radii as manifested by the cluster center-of-mass diffusion coefficients D. For both salts, we find a simple functional form D(c(p), c(s), T) in the parameter range explored. The calculated inter-particle attraction strength, determined from the microscopic and short-time diffusive properties of the samples, increases with salt concentration and temperature in the regime investigated and can be linked to the macroscopic behavior of the samples.
650 7a NATURVETENSKAPx Kemix Fysikalisk kemi0 (SwePub)104022 hsv//swe
650 7a NATURAL SCIENCESx Chemical Sciencesx Physical Chemistry0 (SwePub)104022 hsv//eng
7001 a Grimaldo, Marcou Inst Max von Laue Paul Langevin, 71 Ave Martyrs, F-38042 Grenoble, France.,Institut Laue Langevin4 aut
7001 a Braun, Michal K.u Univ Tubingen, Inst Angew Phys, Morgenstelle 10, D-72076 Tubingen, Germany.,University of Tübingen4 aut
7001 a Buhl, Lenau Univ Tubingen, Inst Angew Phys, Morgenstelle 10, D-72076 Tubingen, Germany.,University of Tübingen4 aut
7001 a Matsarskaia, Olgau Inst Max von Laue Paul Langevin, 71 Ave Martyrs, F-38042 Grenoble, France.,Institut Laue Langevin4 aut
7001 a Jalarvo, Niina H.u Forschungszentrum Julich, Julich Ctr Neutron Sci JCNS, D-52425 Julich, Germany.;Oak Ridge Natl Lab, Chem & Engn Mat Div, Neutron Sci Directorate, POB 2008, Oak Ridge, TN 37831 USA.;Oak Ridge Natl Lab, JCNS Outstn Spallat Neutron Source SNS, POB 2008, Oak Ridge, TN 37831 USA.,Jülich Research Centre,Oak Ridge National Laboratory4 aut
7001 a Zhang, Fajunu Univ Tubingen, Inst Angew Phys, Morgenstelle 10, D-72076 Tubingen, Germany.,University of Tübingen4 aut
7001 a Roosen-Runge, Felixu Malmö University,Lund University,Lunds universitet,Malmö universitet,Institutionen för biomedicinsk vetenskap (BMV),Biofilms Research Center for Biointerfaces,Lund Univ, Div Phys Chem, Nat Vetarvagen 14, S-22100 Lund, Sweden.,Fysikalisk kemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Physical Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)fe2820ro
7001 a Schreiber, Franku Univ Tubingen, Inst Angew Phys, Morgenstelle 10, D-72076 Tubingen, Germany.,University of Tübingen4 aut
7001 a Seydel, Tilou Inst Max von Laue Paul Langevin, 71 Ave Martyrs, F-38042 Grenoble, France.,Institut Laue Langevin4 aut
7102 a Univ Tubingen, Inst Angew Phys, Morgenstelle 10, D-72076 Tubingen, Germany.;Inst Max von Laue Paul Langevin, 71 Ave Martyrs, F-38042 Grenoble, France.b Institut Laue Langevin4 org
7730 t Soft Matterd : Royal Society of Chemistryg :37, s. 8506-8516q :37<8506-8516x 1744-683Xx 1744-6848
8564 u https://doi.org/10.1039/d1sm00418by Fulltext
8564 u https://mau.diva-portal.org/smash/get/diva2:1594191/FULLTEXT01.pdfx primaryx Raw objecty fulltext:print
8564 u https://pubs.rsc.org/en/content/articlepdf/2021/sm/d1sm00418b
8564 u http://dx.doi.org/10.1039/d1sm00418bx freey FULLTEXT
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:mau:diva-45819
8564 8u https://doi.org/10.1039/d1sm00418b
8564 8u https://lup.lub.lu.se/record/1624fe2f-7a90-4617-8a15-b19119a1e3ab

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