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Biophys J, September 2001, p. 1285-1294, Vol. 81, No. 3
*University of Medicine and Pharmacy Timisoara, Department of
Biophysics and Medical Informatics, RO-1900, Timisoara, Romania, and
Institute of Biophysics, Biological Research Center of
the Hungarian Academy of Sciences, H-6701 Szeged, Hungary
The Hofmeister effect consists in changes of protein
solubility triggered by neutral electrolyte cosolutes. Based on the
assumption that salts cause stochastic fluctuations of the free energy
barrier profiles, a kinetic theory of this phenomenon is proposed. An exponentially correlated noise, of amplitude proportional to the salt
concentration, is added to each energy level, and the time-dependence of the mean protein concentration is calculated. It is found that the
theory yields the well-known Setschenow equation if the noise correlation time is low in comparison to the aggregation time constant.
Experimental data on salting-in agents are well fitted, whereas, in the
case of salting-out cosolutes, two independent dichotomic fluctuations
are needed to fit the data. This may result from the fact that, in both
cases, the low-concentration regime is dominated by salting-in
electrostatic contributions, whereas, at high salt concentrations,
electron donor/acceptor interactions become important; these have
opposite effects. The theory offers a novel way to metricate Hofmeister
effects and also leads to thermodynamic quantities, which account for
the influence of salts. The formalism may also be applied to describe
kinetic phenomena in the presence of cosolutes.
Biophys J, September 2001, p. 1285-1294, Vol. 81, No. 3
© 2001 by the Biophysical Society 0006-3495/01/09/1285/10 $2.00
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