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Protein heat capacity reflects the dynamics of enthalpy exchange between the single macromolecule and the surroundings

✍ Scribed by Bernd Hallerbach; Hans-Jürgen Hinz

Publisher
John Wiley and Sons
Year
2000
Tongue
English
Weight
115 KB
Volume
41
Category
Article
ISSN
0887-3585

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✦ Synopsis

Heat capacity has played a prominent role in relating macroscopic and microscopic properties of small molecules and crystals. However, its diagnostic power can also be used for macromolecules such as proteins. It is shown in the present study that the macroscopically observed protein heat capacity provides direct access to the thermodynamic state of the single protein molecule. The new model of the physical basis of protein heat capacity emphasizes the dynamic nature of protein molecules. It incorporates equilibrium fluctuations as an integral constituent and shows that the increase in the magnitude of equilibrium fluctuations is coupled to an increase in the enthalpy flux between the individual protein molecule and its surroundings.

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