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

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

doi:10.1021/acs.jpclett.5b01073

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

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

Research output: Contribution to journal › Article › peer-review

34 Scopus citations

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 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. The finding corroborates the predictive power of the description of proteins as colloids with distinct attractive ion-activated surface patches.

Original language	English
Pages (from-to)	2577-2582
Number of pages	6
Journal	Journal of Physical Chemistry Letters
Volume	6
Issue number	13
DOIs	https://doi.org/10.1021/acs.jpclett.5b01073
State	Published - Jun 19 2015
Externally published	Yes

Keywords

"patchy" colloids
cluster formation
neutron spectroscopy
protein dynamics
self-assembly

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10.1021/acs.jpclett.5b01073

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

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AU - Grimaldo, Marco

AU - Roosen-Runge, Felix

AU - Hennig, Marcus

AU - Zanini, Fabio

AU - Zhang, Fajun

AU - Zamponi, Michaela

AU - Jalarvo, Niina

AU - Schreiber, Frank

AU - Seydel, Tilo

PY - 2015/6/19

Y1 - 2015/6/19

N2 - 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.

AB - 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.

KW - "patchy" colloids

KW - cluster formation

KW - neutron spectroscopy

KW - protein dynamics

KW - self-assembly

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JF - Journal of Physical Chemistry Letters

IS - 13

ER -

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

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Keywords

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