Osmotic stress, crowding, preferential hydration, and binding: A comparison of perspectives.

There has been much confusion recently about the relative merits of different approaches, osmotic stress, preferential interaction, and crowding, to describe the indirect effect of solutes on macromolecular conformations and reactions. To strengthen all interpretations of measurements and to forestall further unnecessary conceptual or linguistic confusion, we show here how the different perspectives all can be reconciled. Our approach is through the Gibbs-Duhem relation, the universal constraint on the number of ways it is possible to change the temperature, pressure, and chemical potentials of the several components in any thermodynamically defined system. From this general Gibbs-Duhem equation, it is possible to see the equivalence of the different perspectives and even to show the precise identity of the more specialized equations that the different approaches use.

[1]  M. Record,et al.  Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: a practical guide to recognizing and interpreting polyelectrolyte effects, Hofmeister effects, and osmotic effects of salts. , 1998, Advances in protein chemistry.

[2]  V. Parsegian,et al.  Reevaluation of chloride's regulation of hemoglobin oxygen uptake: the neglected contribution of protein hydration in allosterism. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[3]  V. Parsegian,et al.  Protein solvation in allosteric regulation: a water effect on hemoglobin. , 1992, Science.

[4]  Sergey M. Bezrukov,et al.  Counting polymers moving through a single ion channel , 1994, Nature.

[5]  D. Rau,et al.  Water release associated with specific binding of gal repressor. , 1995, The EMBO journal.

[6]  E. Grunwald Thermodynamics of molecular species , 1996 .

[7]  R. Bhat,et al.  Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycols , 1992, Protein science : a publication of the Protein Society.

[8]  S. N. Timasheff,et al.  Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. , 1998, Advances in protein chemistry.

[9]  J. Schellman A simple model for solvation in mixed solvents. Applications to the stabilization and destabilization of macromolecular structures. , 1990, Biophysical chemistry.

[10]  S. N. Timasheff In disperse solution, "osmotic stress" is a restricted case of preferential interactions. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[11]  Fumio Oosawa,et al.  Interaction between particles suspended in solutions of macromolecules , 1958 .

[12]  D. Rau,et al.  The B form to Z form transition of poly(dG-m5dC) is sensitive to neutral solutes through an osmotic stress. , 1995, Biochemistry.

[13]  C. Tanford,et al.  Extension of the theory of linked functions to incorporate the effects of protein hydration. , 1969, Journal of molecular biology.

[14]  Sergey M. Bezrukov,et al.  Dynamics and Free Energy of Polymers Partitioning into a Nanoscale Pore , 1996 .

[15]  S. N. Timasheff,et al.  The control of protein stability and association by weak interactions with water: how do solvents affect these processes? , 1993, Annual review of biophysics and biomolecular structure.

[16]  V. Parsegian,et al.  [3] Macromolecules and water: Probing with osmotic stress , 1995 .

[17]  Philip Nelson,et al.  Hard Spheres in Vesicles: Curvature-Induced Forces and Particle-Induced Curvature , 1997, cond-mat/9710016.

[18]  J. Friedman,et al.  Ordered water molecules as key allosteric mediators in a cooperative dimeric hemoglobin. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[19]  D. Rau,et al.  Removing water from an EcoRI-noncognate DNA complex with osmotic stress. , 1999, Journal of biomolecular structure & dynamics.

[20]  D. Winzor,et al.  Thermodynamic nonideality of enzyme solutions supplemented with inert solutes: yeast hexokinase revisited. , 1995, Biophysical chemistry.

[21]  D. Winzor,et al.  Thermodynamic nonideality as a probe of reversible protein unfolding effected by variations in pH and temperature: studies of ribonuclease. , 1990, Archives of biochemistry and biophysics.

[22]  R. Rand,et al.  Probing protein hydration and conformational states in solution. , 1997, Biophysical journal.

[23]  A. Minton,et al.  Molecular crowding: analysis of effects of high concentrations of inert cosolutes on biochemical equilibria and rates in terms of volume exclusion. , 1998, Methods in enzymology.

[24]  H. Eisenberg Protein and nucleic acid hydration and cosolvent interactions: establishment of reliable baseline values at high cosolvent concentrations. , 1994, Biophysical chemistry.

[25]  D. Rau,et al.  Differences in water release for the binding of EcoRI to specific and nonspecific DNA sequences. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[26]  T. Arakawa,et al.  Stabilization of protein structure by sugars. , 1982, Biochemistry.

[27]  V A Parsegian,et al.  Probing alamethicin channels with water-soluble polymers. Size-modulated osmotic action. , 1993, Biophysical journal.

[28]  A. Schechter,et al.  Chemical potential measurements of deoxyhemoglobin S polymerization. Determination of the phase diagram of an assembling protein. , 1985, Journal of molecular biology.

[29]  S. Bezrukov,et al.  Polymeric nonelectrolytes to probe pore geometry: application to the alpha-toxin transmembrane channel. , 1999, Biophysical journal.