The photochromic retinal protein bacteriorhodopsin (BR) was found in the cell membrane of the Archaean Halobacterium salinarium. The excellent photochromic and photocycle properties of the BR provide the possibility of many applications in the filed of optical information processing. In this paper, the spectrum response characteristic of the wild type bacteriorhodopsin molecule film was studied by using pump-probe method. After the samples was excited by 532 nm YAG laser beam, the absorption spectra were probed by an optical fiber spectrum analysis (OSA). The absorption peaks at the ground state (B state) of the two samples are all at 562 nm wavelength. At 562 nm wavelength, the optical densities (OD) of the samples are about OD(WT1)(562 nm...
The protein bacteriorhodopsin (BR) functions as a light-driven proton pump in its native organism Ha...
Picosecond infrared spectroscopy is developed and used for the first time to study the dynamics of p...
The photophysical properties of the retinal-binding proteins, rhodopsin, bacteriorhodopsin and selec...
The optical absorption properties of biological protein bacteriorhodopsin (bR) under the illuminatio...
The optical absorption properties of biological protein bacteriorhodopsin (bR) under the illuminatio...
The optical absorption properties of biological protein bacteriorhodopsin (bR) under the illuminatio...
The optical absorption properties of biological protein bacteriorhodopsin (bR) under the illuminatio...
The bacteriorhodopsin molecule absorbs light and undergoes a series of structural transformation fol...
Bacteriorhodopsin (BR) is a purple trans-membrane protein which constitutes the color and biological...
Abstract. The bacteriorhodopsin molecule absorbs light and undergoes a series of structural trans-fo...
The object of this study is the processes of interaction of fragments of purple membranes with certa...
The wavelength-dependent refractive index of a bacteriorhodopsin thin film is measured by the use of...
Bacteriorhodopsin (BR) is a retinal-binding protein in the purple membrane of Halobacteria where it ...
The protein bacteriorhodopsin (BR) functions as a light-driven proton pump in its native organism Ha...
The protein bacteriorhodopsin (BR) functions as a light-driven proton pump in its native organism Ha...
The protein bacteriorhodopsin (BR) functions as a light-driven proton pump in its native organism Ha...
Picosecond infrared spectroscopy is developed and used for the first time to study the dynamics of p...
The photophysical properties of the retinal-binding proteins, rhodopsin, bacteriorhodopsin and selec...
The optical absorption properties of biological protein bacteriorhodopsin (bR) under the illuminatio...
The optical absorption properties of biological protein bacteriorhodopsin (bR) under the illuminatio...
The optical absorption properties of biological protein bacteriorhodopsin (bR) under the illuminatio...
The optical absorption properties of biological protein bacteriorhodopsin (bR) under the illuminatio...
The bacteriorhodopsin molecule absorbs light and undergoes a series of structural transformation fol...
Bacteriorhodopsin (BR) is a purple trans-membrane protein which constitutes the color and biological...
Abstract. The bacteriorhodopsin molecule absorbs light and undergoes a series of structural trans-fo...
The object of this study is the processes of interaction of fragments of purple membranes with certa...
The wavelength-dependent refractive index of a bacteriorhodopsin thin film is measured by the use of...
Bacteriorhodopsin (BR) is a retinal-binding protein in the purple membrane of Halobacteria where it ...
The protein bacteriorhodopsin (BR) functions as a light-driven proton pump in its native organism Ha...
The protein bacteriorhodopsin (BR) functions as a light-driven proton pump in its native organism Ha...
The protein bacteriorhodopsin (BR) functions as a light-driven proton pump in its native organism Ha...
Picosecond infrared spectroscopy is developed and used for the first time to study the dynamics of p...
The photophysical properties of the retinal-binding proteins, rhodopsin, bacteriorhodopsin and selec...