ArticleProtein science : a publication of the Protein Society2024
Quantitative entropy-enthalpy compensation in intraprotein interactions from model compound data.
Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- UsingMagnetic resonance letters · 2027Article
- Quantitative entropy-enthalpy compensation in intraprotein interactions from model compound data.Protein science : a publication of the Protein Society · 2024Article
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Authors and funding
2 authors.
Funding
Abstract
Many small globular proteins exist in only two states-the physiologically relevant folded state and an inactive unfolded state. The active state is stabilized by numerous weak attractive contacts, including hydrogen bonds, other polar interactions, and the hydrophobic effect. Knowledge of these interactions is key to understanding the fundamental equilibrium thermodynamics of protein folding and stability. We focus on one such interaction, that between amide and aromatic groups. We provide a statistically convincing case for quantitative, linear entropy-enthalpy compensation in forming aromatic-amide interactions using published model compound transfer-free energy data.
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Registered trials
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