Thermodynamic Properties of Proteins

Abstract

This chapter discusses thermodynamic properties like heat capacity, partial volume and thermodynamic function, of proteins. The proteins are heteropolymers consisting of 20 different types of amino acid residues. Molar heat capacities of solid amino acids and polyamino acids, specific heat capacities of anhydrous and hydrated proteins are tabulated. All of the measurements were done by using adiabatic absolute calorimetry. The heat capacity of anhydrous proteins can be predicted using empirical approach developed by Wunderlich. The partial specific volume of proteins can be measured experimentally or can be estimated from the amino acid composition of the protein using statistical equation. Temperature dependence of the partial molar volumes and the partial molar heat capacities of a peptide unit and of the side chains of amino acid residues are listed. The contribution of solvent (water) to the observed changes of thermodynamic parameters of proteins can be assumed to be proportional to the changes in water accessible surface area of the protein groups. Hydration effects were determined by the transfer of model compounds from the gaseous phase to water. The heat capacities of proteins in the native and unfolded states and the heat capacity change upon unfolding are presented. Enthalpy, entropy, and Gibbs energy changes upon the unfolding are listed.

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Title
Thermodynamic Properties of Proteins
Book Title
Physical Properties of Polymers Handbook
Book DOI
10.1007/978-0-387-69002-5
Chapter DOI
10.1007/978-0-387-69002-5_8
Part of
Volume
Editors
  • James E. Mark Send Email (1)
  • Editor Affiliation
  • 1 Department of Chemistry, University of Cincinnati, Crosley Tower, Martin Luther King Drive, 45221-0172, Cincinnati, OH
  • Authors
  • George I. Makhatadze Send Email (2)
  • Author Affiliation
  • 2 Department of Biochemistry and Molecular Biology, Penn State University College of Medicine, 17033, Hershey, PA
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