The salting-out effect of simple electrolytes on lysozyme has been studied by measuring the second virial coefficient B-2 Of the osmotic pressure as a function of salt concentration, and for different salts. The aim of this work has been to End 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-2 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-2. The significance of these findings for the investigation-of protein interactions near crystallization is discussed.

Protein interactions near crystallization: a microscopic approach to the Hofmeister series

PIERNO, MATTEO AMBROGIO PAOLO
2000

Abstract

The salting-out effect of simple electrolytes on lysozyme has been studied by measuring the second virial coefficient B-2 Of the osmotic pressure as a function of salt concentration, and for different salts. The aim of this work has been to End 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-2 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-2. The significance of these findings for the investigation-of protein interactions near crystallization is discussed.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11577/153497
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