The photodynamics of bacteriorhodopsin were studied by transient absorption and gain measurements after excitation with femtosecond pulses at 620 nm. With probing pulses at longer wavelengths (A> 770 nm) the previously reported formation of the J intermediate (with a time constant of 500f 100 fs) was confirmed. With probing pulses around 700 nm, a faster process with a relaxation time of 200 rt...

The membrane protein bacteriorhodopsin contains all-trans-retinal in a binding site lined by amino acid side groups and water molecules that guide the photodynamics of retinal. Upon absorption of light, retinal undergoes a subpicosecond all-trans-->13-cis phototransformation involving torsion around a double bond. The main reaction product triggers later events in the protein that induce pumpin...

Three membrane proteins, OmpF porin from Escherichia coli, bacteriorhodopsin from Halobacterium salinarium, and the hexagonally packed intermediate (HPI) layer from Deinoccocus radiodurans, were investigated with the atomic force microscope in buffer solution. A resolution of up to 0.8 nm allowed structural differences of individual proteins to be detected. OmpF porin exhibits different static ...

All-optical, mirrorless switching and bistability is demonstrated with bacteriorhodopsin (bR). A low-power, 532 nm laser beam modulates the transmission of a cw laser beam at 635 nm that corresponds to peak absorption of the Oexcited state in the bR photocycle. The switch has features like a NOT-gate; its switching contrast depends on the pulse width and average power of the modulating laser. T...