Themed collection Time-resolved methods in biophysics series

The implementation of time-resolved FT-IR spectroscopy to the structural study of membrane proteins and their catalytic mechanisms offers complementary information to other structurally sensitive methods like NMR spectroscopy and X-ray crystallography.

This perspective reviews the physical principles of the laser T-jump methodology, practical experimental considerations and specific applications of the laser T-jump to the broad range of problems in biomolecular dynamics.

This review focuses on the development and modern implementation of the frequency domain approach to time-resolved fluorescence and its application to intrinsic protein fluorescence.

Ultra-sensitive photon counting techniques are able to resolve nanosecond lifetimes of singlet oxygen O₂(a¹Δ_g), even in the presence of strong background luminescence signals, and to reliably measure quantum yields of O₂(a¹Δ_g) production below 0.001.

Time-resolved Laue diffraction is particularly suitable for studying short-lived intermediates in light-sensitive proteins that can be repeatedly excited.

Femtosecond mid-infrared spectroscopy (right) combined with femtosecond visible spectroscopy (left) reveals environmental details of the chlorophylls involved in energy transfer in the light harvesting pigment–protein complexes CP43 and CP47.

A femtosecond pump–probe system based on two synchronized NOPAs that can be independently configured to run either in the visible or in the near-IR frequency range is described.

A thorough introduction into the recently developed fluorescence lifetime correlation spectroscopy.

Nanosecond laser flash photolysis can be exploited to monitor ligand binding kinetics to haem proteins, highlighting ligand migration processes and protein dynamics.

A time-resolved surface-enhanced resonance Raman spectroscopic method is presented that allows for studying electric-field effects on the light-induced reaction cycles of photoreceptors.