Hydrophobic Interactions in Purification and Utilization of Enzymes

  • Wayne Melander
  • Csaba Horvath


The importance of the hydrophobic effect in biochemical systems has been widely recognized since Kauzmann (1) enunciated its role in determining the threedimensional structure of proteins. The strength of hydrophobic interactions is commensurate with that of hydrogen binding and ionic effects in a typical protein (2). Numerous authors have looked for a quantitative ranking for the hydrophobic character of amino acid side chains to estimate the hydrophobicity of proteins (3–6). One theory attributed the large entropy effect to changes in the hydrogen bonding structure of water in the vicinity of solute molecules(7–10); while another found the free energy of hydrocarbons in water to be proportional to the number of solvent molecules surrounding the solute and also to the solute surface area as determined from molecular models (11–14).


Hydrophobic Interaction Adenosine Deaminase Hydrophobic Effect Constant Ionic Strength Hydrogen Bonding Structure 
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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Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • Wayne Melander
    • 1
  • Csaba Horvath
    • 1
  1. 1.Department of Engineering and Applied ScienceYale UniversityNew HavenUSA

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