ArticleRSC chemical biology2020
Enhancing the enthalpic contribution of hydrogen bonds by solvent shielding.
Article in RSC chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 15 citations in OpenAlex.
- Does size matter? - Comparing pyranoses with septanoses as ligands of the bacterial lectin FimH.European journal of medicinal chemistry · 2024Article
- Inhibitor design for TMPRSS2: insights from computational analysis of its backbone hydrogen bonds using a simple descriptor.European biophysics journal : EBJ · 2024Article
- Investigating the Impact of Hydrophobic Polymer Segments on the Self-Assembly Behavior of Supramolecular Cyclic Peptide Systems via Asymmetric-Flow Field Flow Fractionation.Macromolecules · 2023Article
- Structural and biochemical characterization of the relaxosome auxiliary proteins encoded on theComputational and structural biotechnology journal · 2022Article
- Preparation and DFT Study for New Three-Ring Supramolecular H-Bonded Induced Liquid Crystal Complexes.Frontiers in chemistry · 2021Article
Corrections and comments
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Authors and funding
11 authors at 1 institution in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In biological systems, polar interactions are heavily burdened by high desolvation penalties resulting from strong solute-solvent interactions. As a consequence thereof, enthalpic contributions of hydrogen bonds to the free energy of binding are severely diminished. However, this effect is strongly attenuated for interactions within solvent-shielded areas of proteins. In microcalorimetric experiments, we show that the bacterial lectin FimH utilizes conformational adaptions to effectively shield its binding site from solvent. The transition into a lower dielectric environment results in an enthalpic benefit of approximately -13 kJ mol
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Registered trials
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