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EnglishThe 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.
| Titolo: | Protein interactions near crystallization: a microscopic approach to the Hofmeister series | |
| Autori: | ||
| Data di pubblicazione: | 2000 | |
| Rivista: | ||
| 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. | |
| Handle: | http://hdl.handle.net/11577/153497 | |
| Appare nelle tipologie: | 01.01 - Articolo in rivista |
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