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Heat capacity of solid state proteins

I. Thermal analysis

  • Biological/Life Sciences
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Abstract

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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Author information

Authors and Affiliations

  1. Department of Chemistry, University of Tennessee, 37996-I600, Knoxville, TN, USA

    G. Zhang & B. Wunderlich

  2. Division of Analytical and Chemical Sciences, ORNL, 37831-6197, Oak Ridge, TN, USA

    G. Zhang & B. Wunderlich

Authors
  1. G. Zhang
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  2. B. Wunderlich
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Additional information

This work was supported by the Division of Materials Research, NSF, Polymers Program, Grant # DMR 90-00520 and the Division of Materials Sciences, Office of Basic Energy Sciences, DOE, under Contract number DE-AC05-84OR21400 with Lockheed Martin Energy Systems, Inc.

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Zhang, G., Wunderlich, B. Heat capacity of solid state proteins. Journal of Thermal Analysis 49, 823–829 (1997). https://doi.org/10.1007/BF01996766

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