Imaging the membrane protein bacteriorhodopsin with the atomic force microscope
- Univ. of California, Santa Barbara (USA)
The membrane protein bacteriorhodopsin was imaged in buffer solution at room temperature with the atomic force microscope. Three different substrates were used: mica, silanized glass and lipid bilayers. Single bacteriorhodopsin molecules could be imaged in purple membranes adsorbed to mica. A depression was observed between the bacteriorhodopsin molecules. The two dimensional Fourier transform showed the hexagonal lattice with a lattice constant of 6.21 +/- 0.20 nm which is in agreement with results of electron diffraction experiments. Spots at a resolution of approximately 1.1 nm could be resolved. A protein, cationic ferritin, could be imaged bound to the purple membranes on glass which was silanized with aminopropyltriethoxysilane. This opens the possibility of studying receptor/ligand binding under native conditions. In addition, purple membranes bound to a lipid bilayer were imaged. These images may help in interpreting results of functional studies done with purple membranes adsorbed to black lipid membranes.
- OSTI ID:
- 6010923
- Journal Information:
- Biophysical Journal; (USA), Vol. 58:6; ISSN 0006-3495
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
14 SOLAR ENERGY
RHODOPSIN
ELECTRON MICROPROBE ANALYSIS
ADSORPTION
FOURIER TRANSFORMATION
MEMBRANE PROTEINS
PHOTOSYNTHETIC MEMBRANES
SUBSTRATES
CHEMICAL ANALYSIS
INTEGRAL TRANSFORMATIONS
MEMBRANES
MICROANALYSIS
ORGANIC COMPOUNDS
PIGMENTS
PROTEINS
SORPTION
TRANSFORMATIONS
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