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

Grimaldo, Marco; Roosen-Runge, Felix; Hennig, Marcus; Zanini, Fabio; Zhang, Fajun; Zamponi, Michaela; Jalarvo, Niina; Schreiber, Frank; Seydel, Tilo

doi:10.1021/acs.jpclett.5b01073

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

Journal Article · Wed Jun 17 00:00:00 EDT 2015 · Journal of Physical Chemistry Letters

DOI:https://doi.org/10.1021/acs.jpclett.5b01073· OSTI ID:1261447

Grimaldo, Marco ^[1]; Roosen-Runge, Felix ^[2]; Hennig, Marcus ^[1]; Zanini, Fabio ^[3]; Zhang, Fajun ^[3]; Zamponi, Michaela ^[4]; Jalarvo, Niina ^[5]; Schreiber, Frank ^[3]; Seydel, Tilo ^[2]

Inst. Laue-Langevin (ILL), Grenoble (France); Univ. Tubingen, Tubingen (Germany)
Inst. Laue-Langevin (ILL), Grenoble (France)
Univ. Tubingen, Tubingen (Germany)
Julich Research Centre (Germany). Julich Centre for Neutron Science (JCNS); JCNS Outstation at the MLZ, Garching (Germany)
Julich Research Centre (Germany). Julich Centre for Neutron Science (JCNS); Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Spallation Neutron Source (SNS)

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 c_p and c_s, respectively. We observe that D follows a universal master curve D(c_s,c_p) = D(c_s = 0,c_p) g(c_s/c_p), where D(c_s= 0,c_p) is the diffusion coefficient in the absence of salt and g(c_s/c_p) 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.

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Research Organization:: Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: AC05-00OR22725

OSTI ID:: 1261447

Journal Information:: Journal of Physical Chemistry Letters, Vol. 6, Issue 13; ISSN 1948-7185

Publisher:: American Chemical SocietyCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 29 works

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

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