6533b829fe1ef96bd128af76
RESEARCH PRODUCT
Short hydrogen bonds enhance nonaromatic protein-related fluorescence
J. Axel ZeitlerPhilippa J. WoodhamsGabriele S. Kaminski SchierleGonzalo Diaz MironAmberley D. StephensMichael T. RuggieroElyse M. KleistUriel N. MorzanAli HassanaliLuca GrisantiDan CredgingtonAndrew D. BondSaul T. E. JonesMuhammad Nawaz QaisraniMuhammad Nawaz QaisraniMuhammad Nawaz QaisraniRalph GebauerMariano C. González LebreroEmiliano Polisubject
Chemical transformationOptics and PhotonicsGlutamineIntrinsic fluorescenceMolecular Dynamics SimulationPhotochemistryFluorescenceAb initio molecular dynamicsAmmoniaHumansSingle amino acidshort hydrogen bondDensity Functional TheoryMultidisciplinaryHydrogen bondChemistryintrinsic fluorescenceultraviolet fluorescenceHydrogen BondingConical intersectionFluorescenceBiophysics and Computational BiologyExcited statePhysical Sciences408Peptidesdescription
Significance Intrinsic fluorescence of nonaromatic amino acids is a puzzling phenomenon with an enormous potential in biophotonic applications. The physical origins of this effect, however, remain elusive. Herein, we demonstrate how specific hydrogen bond networks can modulate fluorescence. We highlight the key role played by short hydrogen bonds, present in the protein structure, on the ensuing fluorescence. We provide detailed experimental and molecular evidence to explain these unusual nonaromatic optical properties. Our findings should benefit the design of novel optically active biomaterials for applications in biosensing and imaging.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2021-05-01 | Proceedings of the National Academy of Sciences of the United States of America |