Enhancing the enthalpic contribution of hydrogen bonds by solvent shielding

Cramer, Jonathan and Jiang, Xiaohua and Schönemann, Wojciech and Silbermann, Marleen and Zihlmann, Pascal and Siegrist, Stefan and Fiege, Brigitte and Jakob, Roman Peter and Rabbani, Said and Maier, Timm and Ernst, Beat. (2020) Enhancing the enthalpic contribution of hydrogen bonds by solvent shielding. RSC chemical biology, 1 (4). pp. 281-287.

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Official URL: https://edoc.unibas.ch/84510/

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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; -1; for mannoside binding. However, this effect can be abrogated, if the hydrogen bond network within the binding site is disturbed by deoxygenation of the ligand. Conformational adaption leading to reduced local dielectric constants could represent a general mechanism for proteins to enable enthalpy-driven recognition of polar ligands.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Maier)
UniBasel Contributors:Maier, Timm
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:14 Feb 2022 09:50
Deposited On:14 Feb 2022 09:50

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