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

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• 作者：Marco Grimaldo ; Felix Roosen-Runge ; Marcus Hennig ; Fabio Zanini ; Fajun Zhang ; Michaela Zamponi ; Niina Jalarvo ; Frank Schreiber ; Tilo Seydel
• 刊名：The Journal of Physical Chemistry Letters
• 出版年：2015
• 出版时间：July 2, 2015
• 年：2015
• 卷：6
• 期：13
• 页码：2577-2582
• 全文大小：324K
• ISSN：1948-7185

文摘

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.