Search results for "Intrinsic fluorescence"

showing 2 items of 2 documents

Short hydrogen bonds enhance nonaromatic protein-related fluorescence

2021

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.

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 Sciences408PeptidesProceedings of the National Academy of Sciences of the United States of America
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Research data supporting 'Short hydrogen bonds enhance nonaromatic protein-related fluorescence'

2021

Raw data for experimental figures. Files contain .cif (crystallographic information file) for XRD data of the L-pyro-amm structure. .xlsx file containing spectra for absorption of L-glutamine, L-pyroglutamine and L-pyro-amm. .xlsx file contains spectra for fluorescence excitation and emission collected over 8 days for L-glutamine conversion to L-pyro-amm.

intrinsic fluorescenceUV fluorescenceAbsorption
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