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| Hauptseite > Publikationsdatenbank > Salt-Induced Universal Slowing Down of the Short-Time Self-Diffusion of a Globular Protein in Aqueous Solution |
| Hauptseite > Publikationsdatenbank > Salt-Induced Universal Slowing Down of the Short-Time Self-Diffusion of a Globular Protein in Aqueous Solution |
| Journal Article | FZJ-2015-05813 |
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2015
ACS
Washington, DC
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Please use a persistent id in citations: http://hdl.handle.net/2128/9282 http://hdl.handle.net/2128/9283 doi:10.1021/acs.jpclett.5b01073
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.
Keyword(s): Health and Life (1st) ; Health and Life (1st) ; Soft Condensed Matter (2nd) ; Biology (2nd) ; Chemistry (2nd)
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