Using high-pressure fluorescence as a method to investigate cation-π interactions in model proteins
(English)Manuscript (preprint) (Other academic)
This study uses High Pressure fluorescence to obtain interaction energies of weak cation-πinteractions. Since cation-π interactions are believed to contain an electrostatic component; theywould be sensitive to hydrostatic pressure. It has been established that our two model proteins,W33/K37 & W34/K38, contain cation-π interactions that are located in solvated environments.With the use of high pressure Fluorescence we were able to monitor the disruption of the cation-π interaction as well as determine the interaction energy for both solvent exposed pairs,W33/K37 & W34/K38 pairs. The weak interaction energies were found to be 0.08 ± 0.02 & 0.06± 0.02, respectively.
de novo design proteins, cation-pi interaction, high pressure fluorescence
Research subject Biochemistry
IdentifiersURN: urn:nbn:se:su:diva-102113OAI: oai:DiVA.org:su-102113DiVA: diva2:708118