Jul 2026· Journal of Physical Chemistry B· Vol 130, pp. 7867 - 7875· 0 citations· 74 references
Medicine
TL;DR
The computed C p profile of the unmodified tRNA displayed a well-defined peak consistent with experimentally reported C p thermograms for various tRNAs, and the effects of different monovalent ions, distinct interatomic potentials, and varying melting temperature values on the key thermophysical properties of the tRNA isodecoder were probed.
Abstract
The heat capacity (C p ) is a fundamental thermodynamic property widely used to characterize biomolecular conformational stability. Despite extensive investigations into changes in the heat capacity (ΔC p ) associated with protein folding, these effects remain incompletely characterized in the folding of ribonucleic acid (RNA) molecules. In this work, we report on the thermophysical properties of a transfer RNA (tRNA) isodecoder in its chemically unmodified form as well as two modified forms, each having a distinct chemical modification, N 2,N 2-dimethylguanosine (m2,2G) or N 7-methylguanosine (m7G). The computed C p profile of the unmodified tRNA displayed a well-defined peak consistent with experimentally reported C p thermograms for various tRNAs. Based on the consistency between the computed thermophysical properties and experimental observations, we further probed the effects of different monovalent ions, distinct interatomic potentials, and varying melting temperature values on the key thermophysical properties of the tRNA isodecoder.
The results show that the spectra well-reflect molecular geometry, including changes caused by temperature variation, and the combined spectroscopic and computational methodology can be used as a powerful means to study solution properties of nucleic acids.
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