Solvent Effects on Processes in Aqueous Solutions

  • Arieh Ben-Naim

Abstract

Most of the processes treated in Chapters 2 and 3 and part of 4 were assumed to take place in the vacuum. In reality these processes are usually carried out in a solvent. This is certainly true for biochemical processes such as the binding of oxygen to hemoglobin, the binding of substrate to enzymes, the helix-coil transition, etc. In a simple solvent it is often assumed that the theory itself may be retained except for an appropriate rescaling of the parameters involved. This, in general, is not true for complex solvents such as water. Here, the presence of a solvent might change not only the parameters involved in a specific theory, but also the theory itself. For instance, the PF of a simple Ising model with two-state units and nearest-neighbor interactions can be represented by a 2 × 2 matrix. The same model in a solvent could be affected in two ways. First, if the assumptions of the model can be retained, then only the parameters of the model are changed, e.g., the energies of each state or the interaction energies between nearest neighbors. Second, when the assumptions of the model cannot be retained, then the theory itself must be modified. For instance, if the solvent introduces next-nearest-neighbor correlations then the 2 × 2 matrix will not be sufficient to represent the PF of the system. Higher-order matrices would be necessary to treat the same model in a solvent. In more extreme cases, the 1-D model itself must be abandoned.

Keywords

Gibbs Energy Critical Micelle Concentration Pair Correlation Function Thermodynamic Force Probability Ratio 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Suggested Readings

General introductions to protein structure and properties are

  1. T. E. Creighton, Proteins, Structure and Molecular Principles (W. H. Freeman and Co., New York, 1984 ).Google Scholar
  2. G. E. Schulz and R. H. Schirmer, Principles of Protein Structure ( Springer Verlag, Berlin, 1978 ).Google Scholar
  3. C. R. Cantor and P. R. Schimmel, Biophysical Chemistry (W. H. Freeman and Co., San Francisco. 1980 ).Google Scholar
  4. R. Jaenicke, Prog. Biophys. Mol. Biol. 49, 117 (1987).CrossRefPubMedGoogle Scholar

A recent review of the theoretical and computational aspects of proteins is

  1. C. L. Brooks, M. Karplus, and B. M. Pettit, Proteins: A Theoretical Perspective of Dynamics, Structure and Thermodynamics ( John Wiley and Sons, New York, 1988 ).Google Scholar

Copyright information

© Springer Science+Business Media New York 1992

Authors and Affiliations

  • Arieh Ben-Naim
    • 1
  1. 1.Department of Physical ChemistryThe Hebrew University of JerusalemJerusalemIsrael

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