Location of the carboxyl terminus of bacteriorhodopsin in purple membrane.
Purple membrane samples have been prepared by trypsin digestion to have either 10 or 21 residues removed from the carboxyl terminus of the proteins. Electron diffraction of single membranes and x-ray diffraction of unoriented membrane pellets have been carried out on both these specimens and on native purple membranes. the main conclusion from this work is that the carboxyl terminus is almost entirely disordered, being free to take up many positions, and that its removal does not affect the packing in the crystal. The low resolution x-ray diffraction difference map may also suggest the approximate location of the carboxyl terminus.
D001436:Bacteriorhodopsins; D002338:Carotenoids; D006217:Halobacterium; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation; D013057:Spectrum Analysis; D014357:Trypsin; D014961:X-Ray Diffraction
D010446:Peptide Fragments; D002338:Carotenoids; D001436:Bacteriorhodopsins; D014357:Trypsin