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

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]
  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:
OSTI Identifier:
1261447
Grant/Contract Number:
AC05-00OR22725
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
Research Org:
Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
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