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Temperature and salt controlled tuning of protein clusters
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- Beck, Christian (författare)
- 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 Tübingen
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- Grimaldo, Marco (författare)
- Inst Max von Laue Paul Langevin, 71 Ave Martyrs, F-38042 Grenoble, France.,Institut Laue Langevin
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- Braun, Michal K. (författare)
- Univ Tubingen, Inst Angew Phys, Morgenstelle 10, D-72076 Tubingen, Germany.,University of Tübingen
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- 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)
- 2021
- 2021
- Engelska.
- Ingår i: Soft Matter. - : Royal Society of Chemistry. - 1744-683X .- 1744-6848. ; :37, s. 8506-8516
- Tidskriftsartikel (refereegranskat)
Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Kemi -- Fysikalisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Physical Chemistry (hsv//eng)
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- Beck, Christian
- Grimaldo, Marco
- Braun, Michal K.
- Buhl, Lena
- Matsarskaia, Olg ...
- Jalarvo, Niina H ...
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- Zhang, Fajun
- Roosen-Runge, Fe ...
- Schreiber, Frank
- Seydel, Tilo
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