SwePub
Sök i LIBRIS databas

  Extended search

onr:"swepub:oai:DiVA.org:mau-45819"
 

Search: onr:"swepub:oai:DiVA.org:mau-45819" > Temperature and sal...

  • 1 of 1
  • Previous record
  • Next record
  •    To hitlist
  • Beck, ChristianUniv 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 Tübingen (author)

Temperature and salt controlled tuning of protein clusters

  • Article/chapterEnglish2021

Publisher, publication year, extent ...

  • 2021
  • Royal Society of Chemistry,2021
  • electronicrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:mau-45819
  • https://urn.kb.se/resolve?urn=urn:nbn:se:mau:diva-45819URI
  • https://doi.org/10.1039/d1sm00418bDOI
  • https://lup.lub.lu.se/record/1624fe2f-7a90-4617-8a15-b19119a1e3abURI

Supplementary language notes

  • Language:English
  • Summary in:English

Part of subdatabase

Classification

  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • 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.

Subject headings and genre

Added entries (persons, corporate bodies, meetings, titles ...)

  • Grimaldo, MarcoInst Max von Laue Paul Langevin, 71 Ave Martyrs, F-38042 Grenoble, France.,Institut Laue Langevin (author)
  • Braun, Michal K.Univ Tubingen, Inst Angew Phys, Morgenstelle 10, D-72076 Tubingen, Germany.,University of Tübingen (author)
  • Buhl, LenaUniv Tubingen, Inst Angew Phys, Morgenstelle 10, D-72076 Tubingen, Germany.,University of Tübingen (author)
  • Matsarskaia, OlgaInst Max von Laue Paul Langevin, 71 Ave Martyrs, F-38042 Grenoble, France.,Institut Laue Langevin (author)
  • Jalarvo, Niina H.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.,Oak Ridge National Laboratory,Jülich Research Centre (author)
  • Zhang, FajunUniv Tubingen, Inst Angew Phys, Morgenstelle 10, D-72076 Tubingen, Germany.,University of Tübingen (author)
  • Roosen-Runge, FelixMalmö 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, LTH(Swepub:lu)fe2820ro (author)
  • Schreiber, FrankUniv Tubingen, Inst Angew Phys, Morgenstelle 10, D-72076 Tubingen, Germany.,University of Tübingen (author)
  • Seydel, TiloInst Max von Laue Paul Langevin, 71 Ave Martyrs, F-38042 Grenoble, France.,Institut Laue Langevin (author)
  • 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 (creator_code:org_t)

Related titles

  • In:Soft Matter: Royal Society of Chemistry:37, s. 8506-85161744-683X1744-6848

Internet link

Find in a library

To the university's database

  • 1 of 1
  • Previous record
  • Next record
  •    To hitlist

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Close

Copy and save the link in order to return to this view