Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 125, Issue 34, Pages 9719-9726Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.1c05555
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Funding
- National Science Foundation [CHE-1665271]
- Air Force Office of Scientific Research [FA9550-15-1-0090]
- Physics Frontier Center Program [PHY-1734006]
- National Institutes of Health Molecular Biophysics Training Grant [T32 GM-065103]
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The study measured the heat capacity changes in DNA folding at the single-molecule level and the transition state, finding that the results were consistent with previous literature expectations.
Measurements of the thermodynamic properties of biomolecular folding (Delta G degrees, Delta H degrees, Delta S degrees, etc.) provide a wealth of information on the folding process and have long played a central role in biophysical investigation. In particular, the excess heat capacity of folding (Delta C-P) is crucial, as typically measured in bulk ensemble studies by differential scanning calorimetry (DSC) and isothermal titration calorimetry (ITC). Here, we report the first measurements of Delta C-P at the single-molecule level using the single-molecule fluorescence resonance energy transfer (smFRET) as well as the very first measurements of the heat capacity change associated with achieving the transition state (Delta C-P(double dagger)) for nucleic acid folding. The deoxyribonucleic acid (DNA) hairpin used in these studies exhibits an excess heat capacity for hybridization (Delta C-P = -340 +/- 60 J/mol/K per base pair) consistent with the range of literature expectations (Delta C-P = -100 to -420 J/mol/K per base pair). Furthermore, the measured activation heat capacities (Delta C-P(double dagger)) for such hairpin unfolding are consistent with a folding transition state containing few fully formed base pairs, in agreement with prevailing models of DNA hybridization.
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