Potential of mean force treatment of salt-mediated protein crystallization

Biophysical Journal
D M Soumpasis, Y Georgalis

Abstract

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.

Citations

Oct 19, 2000·Biophysical Chemistry·A M KierzekP Zielenkiewicz
Jun 19, 2001·Biophysical Chemistry·A M Kierzek, P Zielenkiewicz
Mar 5, 2010·The Journal of Physical Chemistry. B·Jeremy D Schmit, Ken A Dill
Mar 4, 2000·Science Progress·Y Georgalis, W Saenger
Jan 30, 1999·The Journal of Peptide Research : Official Journal of the American Peptide Society·M ThuneckeY Georgalis

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