Abstract
The effect of two physiological cosolutes (urea and trimethylamine-N-oxide) and of KCl on the intermolecular interactions in concentrated lysozyme solutions were studied by synchrotron radiation small angle x-ray scattering. The evolution of the structure factors as a function of cosolute and/or salt concentration was modeled using pair potentials following an approach recently described in the literature. It was found that the structure factors for salt and/or cosolute concentration series at a fixed protein concentration can best be described using a variable depth attractive potential and a constant effective charge rather than a constant attractive potential and a variable effective charge as done in previous work. © 2005 by the Biophysical Society.
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CITATION STYLE
Niebuhr, M., & Koch, M. H. J. (2005). Effects of urea and trimethylamine-N-oxide (TMAO) on the interactions of lysozyme in solution. Biophysical Journal, 89(3), 1978–1983. https://doi.org/10.1529/biophysj.105.063859
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