Dr. Igor Chizhov
Institute for Biophysical Chemistry
Hannover Medical School
Phone (+49) 511 532
Fax (+49) 511 532 5966
Investigation of conformational changes that occur during turnover of ATP by myosin and mediate the large changes in the affinity of actin-myosin are important to understand the molecular details of the mechanochemical coupling in the motor proteins. Relaxation techniques such as a pressure jump, temperature jump and flash photolysis are powerful tools for the study of ligand binding and conformational changes of proteins and nucleic acids.
Our laboratory provides a set of the fast spectroscopic techniques based on the nanosecond laser pulses operated in the UV, VIS and IR ranges. Currently, we have established the UV-laser (355 nm) flash photolysis of caged compounds to study the kinetics of nucleotide binding for myosins and recombinant myosin constructs that are available only in μg quantities. The tunable OPO nanosecond laser (400-700 nm) allows an investigation of the relaxation spectral kinetics of photoactive proteins such as rhodopsins, cyto-, phytochromes, etc. The ultrafast T-jump (10 ns rise, 10 degrees amplitude, sustaining time up to 100 s) is based on the heating of sample by IR laser radiation (ca 2 μm) from H2-Stimulated Raman Scattering Converter and cw 15W Thulium Fiber laser. The designed spectrometer allows the detection of the UV-VIS absorption/ fluorescent/light scattering changes within the range 250-800 nm and with the time resolution up to 10 ns.