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ZB 10 - Soft Condensed Matter (R. Holyst)

We are different, but we all do great Science; and we have a lot of fun doing it!
We are different, but we all do great Science; and we have a lot of fun doing it!
We are different, but we all do great Science; and we have a lot of fun doing it!
We are different, but we all do great Science; and we have a lot of fun doing it!
We are different, but we all do great Science; and we have a lot of fun doing it!
We are different, but we all do great Science; and we have a lot of fun doing it!
We are different, but we all do great Science; and we have a lot of fun doing it!
We are different, but we all do great Science; and we have a lot of fun doing it!

Publication

Net charge and electrophoretic mobility of lysozyme charge ladders in solutions of nonionic surfactant

Author(s): Szymanski, Jedrzej and Pobozy, Ewa and Trojanowicz, Marek and Wilk, Agnieszka and Garstecki, Piotr and Holyst, Robert
Title: Net charge and electrophoretic mobility of lysozyme charge ladders in solutions of nonionic surfactant
Abstract: We report on the electrophoretic mobility and on the thermal diffusion lysozyme proteins dissolved in aqueous solutions of a nonionic (C12E6) at a wide range of concentrations of the surfactant by weight). We want to estimate the influence of a dense network elongated micelles of C12E6 on the effective charge of the proteins observed in the capillary electrophoresis experiments. The possible leading to the change in the effective charge of protein could the deformation of the cloud of counterions around the protein it squeezes through the narrow (of the order of a protein diameter) channels formed in the solution of elongated micelles. The of independent measurements of the electrophoretic mobility a family of modified proteins (lysozyme charge ladder [}Colton et J. Am. Chem. Soc. 1997, 119, 12701]), of the microviscosity of the of surfactant (obtained via fluorescence correlation and of the hydrodynamic radius of the proteins (photon spectroscopy) allow us to conclude that the effective charge the proteins is not affected by the presence of surfactant, even at high concentrations.
Pages: 5503-5510
Journal: JOURNAL OF PHYSICAL CHEMISTRY B
Volume: 111
ID: ISI:000246341300064
Year: 2007
DOI: 10.1021/jp067511d