Localization of two chymotryptic fragments in the structure of renatured bacteriorhodopsin by neutron diffraction.
The structure of crystalline purple membrane reconstituted from purified bacteriorhodopsin (BR) chymotryptic fragments has been studied by neutron diffraction. In one of the samples studied, the fragment C-2, encompassing the first two predicted transmembrane segments, was prepared from deuterated purple membrane. The diffraction changes when the natural C-2 fragment is substituted by a deuterated one are analysed in terms of a seven-helix model for BR. The assignment of the labelled fragment to one end of the molecule placed new constraints on folding models for the protein.
D001436:Bacteriorhodopsins / Q000378:metabolism*; D002918:Chymotrypsin; D006217:Halobacterium / Q000378:metabolism; D008958:Models, Molecular; D009501:Neutron Activation Analysis; D010446:Peptide Fragments / Q000378:metabolism; D011487:Protein Conformation; D011489:Protein Denaturation
D010446:Peptide Fragments; D001436:Bacteriorhodopsins; D002918:Chymotrypsin