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Salt-Induced Universal Slowing Down of the Short-Time Self-Diffusion of a Globular Protein in Aqueous Solution

Grimaldo, Marco ; Roosen-Runge, Felix LU ; Hennig, Marcus ; Zanini, Fabio ; Zhang, Fajun ; Zamponi, Michaela ; Jalarvo, Niina ; Schreiber, Frank and Seydel, Tilo (2015) In Journal of Physical Chemistry Letters 6(13). p.2577-2582
Abstract

The short-time self-diffusion D of the globular model protein bovine serum albumin in aqueous (D2O) solutions has been measured comprehensively as a function of the protein and trivalent salt (YCl3) concentration, noted cp and cs, respectively. We observe that D follows a universal master curve D(cs,cp) = D(cs = 0,cp) g(cs/cp), where D(cs = 0,cp) is the diffusion coefficient in the absence of salt and g(cs/cp) is a scalar function solely depending on the ratio of the salt and protein concentration. This observation is consistent with a universal scaling of the bonding probability in a... (More)

The short-time self-diffusion D of the globular model protein bovine serum albumin in aqueous (D2O) solutions has been measured comprehensively as a function of the protein and trivalent salt (YCl3) concentration, noted cp and cs, respectively. We observe that D follows a universal master curve D(cs,cp) = D(cs = 0,cp) g(cs/cp), where D(cs = 0,cp) is the diffusion coefficient in the absence of salt and g(cs/cp) is a scalar function solely depending on the ratio of the salt and protein concentration. This observation is consistent with a universal scaling of the bonding probability in a picture of cluster formation of patchy particles. The finding corroborates the predictive power of the description of proteins as colloids with distinct attractive ion-activated surface patches.

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author
; ; ; ; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
keywords
"patchy" colloids, cluster formation, neutron spectroscopy, protein dynamics, self-assembly
in
Journal of Physical Chemistry Letters
volume
6
issue
13
pages
6 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • scopus:84947754038
  • pmid:26266736
ISSN
1948-7185
DOI
10.1021/acs.jpclett.5b01073
language
English
LU publication?
no
id
f8c12396-53dd-41e8-9493-f4a53378f599
date added to LUP
2018-12-17 09:43:02
date last changed
2025-07-11 02:36:39
@article{f8c12396-53dd-41e8-9493-f4a53378f599,
  abstract     = {{<p>The short-time self-diffusion D of the globular model protein bovine serum albumin in aqueous (D<sub>2</sub>O) solutions has been measured comprehensively as a function of the protein and trivalent salt (YCl<sub>3</sub>) concentration, noted c<sub>p</sub> and c<sub>s</sub>, respectively. We observe that D follows a universal master curve D(c<sub>s</sub>,c<sub>p</sub>) = D(c<sub>s</sub> = 0,c<sub>p</sub>) g(c<sub>s</sub>/c<sub>p</sub>), where D(c<sub>s</sub> = 0,c<sub>p</sub>) is the diffusion coefficient in the absence of salt and g(c<sub>s</sub>/c<sub>p</sub>) is a scalar function solely depending on the ratio of the salt and protein concentration. This observation is consistent with a universal scaling of the bonding probability in a picture of cluster formation of patchy particles. The finding corroborates the predictive power of the description of proteins as colloids with distinct attractive ion-activated surface patches.</p>}},
  author       = {{Grimaldo, Marco and Roosen-Runge, Felix and Hennig, Marcus and Zanini, Fabio and Zhang, Fajun and Zamponi, Michaela and Jalarvo, Niina and Schreiber, Frank and Seydel, Tilo}},
  issn         = {{1948-7185}},
  keywords     = {{"patchy" colloids; cluster formation; neutron spectroscopy; protein dynamics; self-assembly}},
  language     = {{eng}},
  month        = {{06}},
  number       = {{13}},
  pages        = {{2577--2582}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Journal of Physical Chemistry Letters}},
  title        = {{Salt-Induced Universal Slowing Down of the Short-Time Self-Diffusion of a Globular Protein in Aqueous Solution}},
  url          = {{http://dx.doi.org/10.1021/acs.jpclett.5b01073}},
  doi          = {{10.1021/acs.jpclett.5b01073}},
  volume       = {{6}},
  year         = {{2015}},
}