We apply an integrated approach combining microsecond MD simulations and (polarizable)
QM/MM calculations of NMR, FTIR, and UV–vis spectra to validate the structure of the light …

Ultrafast transient infrared (TRIR) spectroscopy is widely used to measure the excitation-
induced structural changes of protein-bound chromophores. Here, we design a novel and …

Photoreceptor proteins bind a chromophore, which, upon light absorption, modifies its
geometry or its interactions with the protein, finally inducing the structural change needed to …

Flavin mononucleotide-binding proteins or domains emit cyan-green fluorescence under
aerobic and anaerobic conditions, but relatively low fluorescence and less thermostability …

Fluorescent proteins (FPs) are biotags of choice for second-harmonic imaging microscopy
(SHIM). Because of their large size, computing their second-harmonic generation (SHG) …

The development of bright fluorescent proteins (FPs) emitting beyond 600 nm continues to
be of interest both from a fundamental perspective in understanding protein-chromophore …

Site-specific protein labeling plays a core role in investigating protein function at molecular
level. A multitude of protein labelling techniques has been developed which are based on …

The photochemistry and photophysics of organic chromophores in photoresponsive proteins
can be tuned by non-covalent protein-chromophore interactions, which are experimentally …

The interplay between light and matter gives rise to several phenomena, including nonlinear
optical (NLO) effects. This thesis aims at describing and understanding, using quantum …