Published In
Biochemical and Biophysical Research Communications
Document Type
Pre-Print
Publication Date
1-2022
Subjects
DNA replication -- Genomes
Abstract
It has been reported for many globular proteins that the native heat capacity at 25°C, per gram, is the same. This has been interpreted to indicate that heat capacity is a fundamental property of native proteins that provides important information on molecular structure and stability. Heat capacities for both proteins and DNA has been suggested to be related to universal effects of hydration/solvation on native structures. Here we report on results from thermal denaturation analysis of two well-known proteins, human serum albumin and lysozyme, and a short DNA hairpin. The transition heat capacities at the Tm for the three molecules were quantitatively evaluated by differential scanning calorimetry. When normalized per gram rather than per mol the transition heat capacities were found to be precisely equivalent. This observation for the transition heat capacities of the proteins is consistent with previous reports. However, an identical transition heat capacity for DNA has not been reported and was unexpected. Further analysis of the collected data suggested a mass dependence of hydration effects on thermal denaturation that is preserved at the individual protein amino acid and DNA base levels. Equivalence of transition heat capacities suggests the possibility of a universal role of hydration effects on the thermal stability of both proteins and DNA.
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DOI
10.1101/2021.12.29.474479
Persistent Identifier
https://archives.pdx.edu/ds/psu/37072
Citation Details
Published as: Eskew, M. W., & Benight, A. S. (2022). Equivalence of the transition heat capacities of proteins and DNA. Biochemical and Biophysical Research Communications.
Description
This is the author’s version of a work. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document.
bioRxiv preprint doi: https://doi.org/10.1101/2021.12.29.474479; this version posted December 30, 2021. The copyright holder for this preprint available under a CC-BY-NC-ND 4.0 International license. (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made