0000000000656687
AUTHOR
Gonzalo Diaz Miron
showing 3 related works from this author
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.
Short hydrogen bonds enhance non-aromatic protein-related fluorescence
2020
AbstractFluorescence in biological systems is usually associated with the presence of aromatic groups. Here, we show that specific hydrogen bonding networks can significantly affect fluorescence employing a combined experimental and computational approach. In particular, we reveal that the single amino acid L-glutamine, by undergoing a chemical transformation leading to the formation of a short hydrogen bond, displays optical properties that are significantly enhanced compared to L-glutamine itself. Ab initio molecular dynamics simulations highlight that these short hydrogen bonds prevent the appearance of a conical intersection between the excited and the ground states and thereby signific…
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.