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

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 picture of cluster formation of patchy particles. In conclusion, the finding corroborates the predictive power of the description of proteins as colloids with distinct attractive ion-activated surface patches.

Authors:
 [1];  [2];  [1];  [3];  [3];  [4];  [5];  [3];  [2]
+ Show Author Affiliations
  1. Inst. Laue-Langevin (ILL), Grenoble (France); Univ. Tubingen, Tubingen (Germany)
  2. Inst. Laue-Langevin (ILL), Grenoble (France)
  3. Univ. Tubingen, Tubingen (Germany)
  4. Julich Research Centre (Germany). Julich Centre for Neutron Science (JCNS); JCNS Outstation at the MLZ, Garching (Germany)
  5. Julich Research Centre (Germany). Julich Centre for Neutron Science (JCNS); Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Spallation Neutron Source (SNS)
Publication Date:
Research Org.:
Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
OSTI Identifier:
1261447
Grant/Contract Number:  
AC05-00OR22725
Resource Type:
Accepted Manuscript
Journal Name:
Journal of Physical Chemistry Letters
Additional Journal Information:
Journal Volume: 6; Journal Issue: 13; Journal ID: ISSN 1948-7185
Publisher:
American Chemical Society
Country of Publication:
United States
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; cluster formation; neutron spectroscopy; protein dynamics; self-assembly; “patchy” colloids

Citation Formats

Grimaldo, Marco, Roosen-Runge, Felix, Hennig, Marcus, Zanini, Fabio, Zhang, Fajun, Zamponi, Michaela, Jalarvo, Niina, Schreiber, Frank, and Seydel, Tilo. Salt-Induced Universal Slowing Down of the Short-Time Self-Diffusion of a Globular Protein in Aqueous Solution. United States: N. p., 2015. Web. doi:10.1021/acs.jpclett.5b01073.
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Grimaldo, Marco, Roosen-Runge, Felix, Hennig, Marcus, Zanini, Fabio, Zhang, Fajun, Zamponi, Michaela, Jalarvo, Niina, Schreiber, Frank, & Seydel, Tilo. Salt-Induced Universal Slowing Down of the Short-Time Self-Diffusion of a Globular Protein in Aqueous Solution. United States. https://doi.org/10.1021/acs.jpclett.5b01073
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Grimaldo, Marco, Roosen-Runge, Felix, Hennig, Marcus, Zanini, Fabio, Zhang, Fajun, Zamponi, Michaela, Jalarvo, Niina, Schreiber, Frank, and Seydel, Tilo. Wed . "Salt-Induced Universal Slowing Down of the Short-Time Self-Diffusion of a Globular Protein in Aqueous Solution". United States. https://doi.org/10.1021/acs.jpclett.5b01073. https://www.osti.gov/servlets/purl/1261447.
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@article{osti_1261447,
title = {Salt-Induced Universal Slowing Down of the Short-Time Self-Diffusion of a Globular Protein in Aqueous Solution},
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},
abstractNote = {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. In conclusion, the finding corroborates the predictive power of the description of proteins as colloids with distinct attractive ion-activated surface patches.},
doi = {10.1021/acs.jpclett.5b01073},
journal = {Journal of Physical Chemistry Letters},
number = 13,
volume = 6,
place = {United States},
year = {Wed Jun 17 00:00:00 EDT 2015},
month = {Wed Jun 17 00:00:00 EDT 2015}
}
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https://doi.org/10.1021/acs.jpclett.5b01073
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