%0 Journal Article
%A Grimaldo, Marco
%A Roosen-Runge, Felix
%A Hennig, Marcus
%A Zanini, Fabio
%A Zhang, Fajun
%A Zamponi, Michaela
%A Jalarvo, Niina
%A Schreiber, Frank
%A Seydel, Tilo
%T Salt-Induced Universal Slowing Down of the Short-Time Self-Diffusion of a Globular Protein in Aqueous Solution
%J The journal of physical chemistry letters
%V 6
%N 13
%@ 1948-7185
%C Washington, DC
%I ACS
%M FZJ-2015-05813
%P 2577 - 2582
%D 2015
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000357626700027
%$ pmid:26266736
%R 10.1021/acs.jpclett.5b01073
%U https://juser.fz-juelich.de/record/255680