The photoisomerization reaction of a fluorescent protein chromophore occurs on the ultrafast
timescale. The structural dynamics that result from femtosecond optical excitation have …

Chromophores absorb light in photosensitive proteins and thereby initiate fundamental
biological processes such as photosynthesis, vision and biofluorescence. An important goal …

Chromophore cis/trans photoisomerization is a fundamental process in chemistry and in the
activation of many photosensitive proteins. A major task is understanding the effect of the …

We demonstrate that the methods of quantum control can be applied successfully to very
large molecules in room temperature liquid solution. Chirped femtosecond pulses are used …

▪ Abstract Time-resolved infrared (IR) and Raman spectroscopy elucidates molecular
structure evolution during ultrafast chemical reactions. Following vibrational marker modes …

Femtosecond time-resolved spectroscopy on model peptides with built-in light switches
combined with computer simulation of light-triggered motions offers an attractive integrated …

The catalytic activity of proteins is a function of structural changes. Very often these are as
minute as protonation changes, hydrogen bonding changes, and amino acid side chain …

Correlated motions of proteins are critical to function, but these features are difficult to
resolve using traditional structure determination techniques. Time-resolved X-ray methods …

Light absorption can trigger biologically relevant protein conformational changes. The light-
induced structural rearrangement at the level of a photoexcited chromophore is known to …

Fluorescence spectroscopy of a green fluorescent protein mutant at single-molecule
resolution has revealed a remarkable oscillatory behavior that can also be driven by applied …