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Heat Capacity and Compactness of Denatured Proteins by Themis Lazaridis; Martin Karplus is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Heat Capacity and Compactness of Denatured Proteins about?

One of the striking results of protein thermodynamics is that the heat capacity change upon denaturation is large and positive. This change is generally ascribed to the exposure of non-polar groups to water on denaturation, in analogy to the large heat capacity change for the transfer of small non-polar molecules from hydrocarbons to water. Calculations of the heat capacity based on the exposed surface area of the completely unfolded denatured state give good agreement with experimental data. This result is difficult to reconcile with evidence that the heat denatured state in the absence of denaturants is reasonably compact. In this work, sample conformations for the denatured state of truncated CI2 are obtained by use of an effective energy function for proteins in solution. The energy function gives denatured conformations that are compact with radii of gyration that are slightly larger than that of the native state. The model is used to estimate the heat capacity, as well as that of the native state, at 300 and 350 K via finite enthalpy differences. The calculations show that the heat capacity of denaturation can have large positive contributions from non-covalent intraprotein i

Who reads Heat Capacity and Compactness of Denatured Proteins?

Author

Themis Lazaridis; Martin Karplus

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0301-4622)

Published

1999

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)