ArticleMonatshefte fur chemie2013
Entropy-enthalpy Compensation of Biomolecular Systems in Aqueous Phase: a Dry Perspective.
Article in Monatshefte fur chemie, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- On Enthalpy-Entropy Compensation Characterizing Processes in Aqueous Solution.Entropy (Basel, Switzerland) · 2025Review
- Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.International journal of molecular sciences · 2023Review
- A Thermodynamic Model for Multivalency in 14-3-3 Protein-Protein Interactions.Journal of the American Chemical Society · 2018Article
- Mechanistic insights into temperature-dependent regulation of the simple cyanobacterial hsp17 RNA thermometer at base-pair resolution.Nucleic acids research · 2015Article
- Quasithermodynamic contributions to the fluctuations of a protein nanopore.ACS chemical biology · 2015Article
- Thermodynamic aspects of cAMP dependent protein kinase catalytic subunit allostery.The protein journal · 2014Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
We survey thermodynamic measurements on processes involving biological macromolecules in aqueous solution, which illustrate well the ubiquitous phenomenon of entropy-enthalpy compensation. The processes include protein folding/unfolding and ligand binding/unbinding, with compensation temperatures varying by about 50 K around an average near 293 K. We show that incorporating both near-exact entropy-enthalpy compensation (due to solvent relaxation) and multi-excitation entropy (from vibrational quanta) leads to a compensation temperature in water of about 230 K. We illustrate a general procedure for subtracting solvent and environment-related terms to determine the bare Gibbs free energy changes of chemical processes.
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