Protein interactions near crystallization: a microscopic approach to the Hofmeister series
Roberto Piazza; Matteo Pierno; Roberto Piazza; Istituto Nazionale per la Fisica della Materia, Unitá Pavia and Dipartimento di Ingegneria Nucleare, Politecnico di Milano, via Ponzio 34/3, 20133 Milan, Italy; Matteo Pierno; Istituto Nazionale per la Fisica della Materia, Unitá Pavia and Dipartimento di Ingegneria Nucleare, Politecnico di Milano, via Ponzio 34/3, 20133 Milan, Italy
Журнал:
Journal of Physics: Condensed Matter
Дата:
2000-02-28
Аннотация:
The salting-out effect of simple electrolytes on lysozyme has been studied by measuring the second virial coefficient B <sub>2</sub> of the osmotic pressure as a function of salt concentration, and for different salts. The aim of this work has been to find a microscopic counterpart of the empirical Hofmeister series for the efficiency of cations and anions in inducing protein crystallization. The experimental results show that, for large enough ionic strengths, B <sub>2</sub> scales linearly with the salt concentration. This trend is common to a number of different monovalent salts, however with efficiency strongly dependent on the specific anion. Conversely, changing the cation does not appreciably affect B <sub>2</sub> . The significance of these findings for the investigation of protein interactions near crystallization is discussed.
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