Ultrafast Optical Processes Laboratory
From BTRR
Overview
The resource develops laser-based methods for investigating structures, dynamics, structural changes, and ultrafast processes in biologically relevant samples. Available ultrafast (femtosecond, picosecond, and nanosecond) laser-based methodologies cover the whole spectral range from ultraviolet (UV) to infrared (IR). Phase-controlled IR pulse methods are used and further developed for multidimensional IR spectroscopy for structural and dynamical studies in peptides and proteins; transient spectroscopy (UV/VIS/IR) and multiphoton absorption techniques are used to study electron and energy transfer dynamics, photo-induced processes in light-sensitive biomolecules, and photophysics down to the single molecule level; time-correlated single-photon counting is used for fluorescence lifetime measurements; laser-induced temperature jumps are used to study protein-folding dynamics; and (time-resolved) confocal and total internal reflection fluorescence microscopy is used to study the diffusion and dynamics of single biomolecules and their complexes in various environments, including vesicles and cells.
Current Research
Two-dimensional IR spectroscopy (IR analogues of nuclear magnetic resonance) to study the dynamics of structures occurring in proteins and peptides; coherent IR methods to examine structural fluctuations through vibrational correlation functions; IR/VIS pump-probe methods with vibrational mode selectivity to study (vibrational) dynamics, mode coupling, and energy transfer; transient IR/VIS probing of protein folding and conformational dynamics through the application of T-jump, stopped-flow, and isotope-editing techniques; time- and frequency-resolved spectroscopy of single proteins and biological assemblies, including the application of lifetime imaging and fluorescence resonance energy transfer techniques in combination with confocal microscopy; and total internal reflection microscopy of single molecules in living cells and large lipid vesicles.
