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Generic pathways to stability in concentrated protein mixtures
Voets, Ilja K.
Institute for Complex Molecular Systems and Laboratory of Macromolecular and Organic Chemistry, Eindhoven University of Technology, The Netherlands - Adolphe Merkle Institute, University of Fribourg, Switzerland
Department of Physics, University of Fribourg, Switzerland
Division of Physical Chemistry, Center for Chemistry and Chemical Engineering, Lund University, Sweden
- Physical Chemistry Chemical Physics. - 2012, vol. 14, no. 8, p. 2929-2933
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.
- Faculté des sciences et de médecine
- Département de Physique, AMI - Soft Nanoscience
- tra_gps.pdf: 18
- tra_gps_sm.pdf: 13