Potential of mean force treatment of salt-mediated protein crystallization

DM Soumpasis, Y Georgalis - Biophysical journal, 1997 - cell.com
DM Soumpasis, Y Georgalis
Biophysical journal, 1997cell.com
In the initial stages of crystallization of proteins, monomers aggregate rapidly and form
nuclei and large fractal clusters, as previously shown by dynamic light scattering
experiments (Georgalis, Y., J. Schüler, J. Frank, DM Soumpasis, and W. Saenger. 1995.
Protein crystallization screening through scattering techniques. Adv. Colloid Interface Sci.
58: 57–86). In this communication we initiate an effort to understand the effective interactions
controlling charged protein aggregation and crystallization using the potential of mean force …
In the initial stages of crystallization of proteins, monomers aggregate rapidly and form nuclei and large fractal clusters, as previously shown by dynamic light scattering experiments (Georgalis, Y., J. Schüler, J. Frank, D. M. Soumpasis, and W. Saenger. 1995. Protein crystallization screening through scattering techniques. Adv. Colloid Interface Sci. 58:57–86). In this communication we initiate an effort to understand the effective interactions controlling charged protein aggregation and crystallization using the potential of mean force (PMF) theory. We compute the PMFs of the system lysozyme-water-NaCl within the framework of the hypernetted chain approximation for a wide range of protein and salt concentrations. We show that the computed effective interactions can rationalize the experimentally observed aggregation behavior of lysozyme under crystallization conditions.
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