Authors: G. Zhang and B. Wunderlich
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  • 1 Department of Chemistry, University of Tennessee, 37996-I600 Knoxville, TN USA
  • | 2 Division of Analytical and Chemical Sciences, ORNL, 37831-6197 Oak Ridge, TN USA
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In an ongoing effort to understand the thermodynamic properties of proteins, ovalbumin, lactoglobulin, lysozyme are studied by adiabatic and differential scanning calorimetry over wide temperature ranges. The heat capacities of the samples in their pure, solid states are linked to an approximate vibrational spectrum with the ATHAS analysis that makes use of known group vibrations and a set of parameters, Θ1 and Θ3, of the Tarasov function for the skeletal vibrations. Good agreement is found between experiment and calculation with rms errors mostly within ±3%. The analyses were also carried out with an empirical addition scheme using data from polypeptides of naturally occurring amino acids. Due to space limitation, only selected results are reported.

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