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

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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.


  • Marco Grimaldo
  • Felix Roosen-Runge
  • Marcus Hennig
  • Fabio Zanini
  • Fajun Zhang
  • Michaela Zamponi
  • Niina Jalarvo
  • Frank Schreiber
  • Tilo Seydel
Externa organisationer
  • Institut Laue Langevin
  • University of Tübingen
  • Max Planck Institute for Developmental Biology
  • Jülich Research Centre
  • Oak Ridge National Laboratory


Sidor (från-till)2577-2582
Antal sidor6
TidskriftJournal of Physical Chemistry Letters
Utgåva nummer13
StatusPublished - 2015 jun 19
Peer review utfördJa
Externt publiceradJa