Salt-Induced Universal Slowing Down of the Short-Time Self-Diffusion of a Globular Protein in Aqueous Solution
Résumé
The short-time self-diffusion D of the globular model protein bovine serum albumin in aqueous (D 2O) solutions has been measured comprehensively as a function of the protein and trivalent salt (YCl 3 ) 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.
Domaines
Matière Molle [cond-mat.soft]| Origine | Fichiers produits par l'(les) auteur(s) |
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