Controlling the activity of proteins with azobenzene photoswitches is a potent tool for
manipulating their biological function. With the help of light, it is possible to change binding …

We present a detailed discussion of the complimentary fields of the application of two-
dimensional infrared (2D-IR) spectroscopy in comparison with two-dimensional nuclear …

By covalently linking an azobenzene photoswitch across the binding groove of a PDZ
domain, a conformational transition, similar to the one occurring upon ligand binding to the …

Two cyclic disulfide-bridged tetrapeptides [cyclo (Boc-Cys-Pro-Aib-Cys-OMe)(1) and cyclo
(Boc-Cys-Pro-Phe-Cys-OMe)(2)] have been monitored by time-resolved mid-IR …

We have run trajectory surface hopping simulations of the trans→ cis photoisomerization of
azobenzene, subject to a pulling force. The model mimics two situations: a trans …

The dynamics of peptide–protein binding and unbinding of a variant of the RNase S system
has been investigated. To initiate the process, a photoswitchable azobenzene moiety has …

The character and dynamics of low-lying electronic excited states of the complexes fac-[Re
(Cl)(CO) 3 (papy) 2] and fac-[Re (papy)(CO) 3 (bpy)]+(papy= trans-4-phenylazopyridine) …

The first steps of the photocycle of the D97N mutant of proteorhodopsin (PR) have been
investigated by means of ultrafast transient absorption spectroscopy. A comparison with the …

The photoresponsive polypeptides discussed in this chapter are obtained by introducing
photochromic units, such as azobenzene or spiropyran groups, into the macromolecules …

Photoswitches suitably connected to model peptides allow to apply light as trigger for folding
initiation. Time-resolved infrared spectroscopy provides a certain degree of structural …