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ABSTRACT:
SUBMITTER: Cramer J
PROVIDER: S-EPMC8341794 | biostudies-literature | 2020 Oct
REPOSITORIES: biostudies-literature
Cramer Jonathan J Jiang Xiaohua X Schönemann Wojciech W Silbermann Marleen M Zihlmann Pascal P Siegrist Stefan S Fiege Brigitte B Jakob Roman Peter RP Rabbani Said S Maier Timm T Ernst Beat B
RSC chemical biology 20200828 4
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 ...[more]