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Issue 8, 2012
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Generic pathways to stability in concentrated protein mixtures

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Abstract

We present a series of experimental results that disclose the crucial role of ionic strength and partial volume fractions in the control of the phase behaviour of binary protein mixtures. Our findings can be understood as that the ionic strength determines the relative contribution of the entropy of the protein counter-ions to the overall thermodynamics of the system. Associative phase separation and crystallization observed at, respectively, low and high ionic strength are suppressed at intermediate salt concentrations, where the entropy gain upon releasing the counter-ions from the double layer of the proteins is negligible and the entropy loss upon confining the counter-ions within the protein crystal phase significant. Moreover, we find that the partial volume fraction of the protein prone to crystallize determines the crystallization boundary and that the presence of other proteins strongly delays crystallization, leading to temporarily stable mixtures. These findings suggest that stability in more complex protein mixtures, such as the cytosol, relates to the ionic strength and protein composition rather than to protein specific properties.

Graphical abstract: Generic pathways to stability in concentrated protein mixtures

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Publication details

The article was received on 08 Aug 2011, accepted on 12 Dec 2011 and first published on 19 Jan 2012


Article type: Paper
DOI: 10.1039/C2CP22558A
Citation: Phys. Chem. Chem. Phys., 2012,14, 2929-2933
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    Generic pathways to stability in concentrated protein mixtures

    I. K. Voets, V. Trappe and P. Schurtenberger, Phys. Chem. Chem. Phys., 2012, 14, 2929
    DOI: 10.1039/C2CP22558A

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