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| 024 | 7 | _ | |a 10.1021/acs.jpclett.5b01073 |2 doi |
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| 100 | 1 | _ | |a Grimaldo, Marco |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Salt-Induced Universal Slowing Down of the Short-Time Self-Diffusion of a Globular Protein in Aqueous Solution |
| 260 | _ | _ | |a Washington, DC |c 2015 |b ACS |
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| 520 | _ | _ | |a 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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| 773 | _ | _ | |a 10.1021/acs.jpclett.5b01073 |g Vol. 6, no. 13, p. 2577 - 2582 |0 PERI:(DE-600)2522838-9 |n 13 |p 2577 - 2582 |t The @journal of physical chemistry letters |v 6 |y 2015 |x 1948-7185 |
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