Irreversible conformational change of bacterio-opsin induced by binding of retinal during its reconstitution to bacteriorhodopsin, as studied by (13)C NMR.

@article{Yamaguchi2000IrreversibleCC,
  title={Irreversible conformational change of bacterio-opsin induced by binding of retinal during its reconstitution to bacteriorhodopsin, as studied by (13)C NMR.},
  author={Satoru Yamaguchi and Satoru Tuzi and Michikazu Tanio and Akira Naito and Janos K. Lanyi and Richard Needleman and Hazime Sait{\^o}},
  journal={Journal of biochemistry},
  year={2000},
  volume={127 5},
  pages={861-9}
}
We compared (13)C NMR spectra of [3-(13)C]Ala- and [1-(13)C]Val-labeled bacterio-opsin (bO), produced either by bleaching bR with hydroxylamine or from a retinal-deficient strain, with those of bacteriorhodopsin (bR), in order to gain insight into the conformational changes of the protein backbone that lead to correct folding after retinal is added to bO. The observed (13)C NMR spectrum of bO produced by bleaching is not greatly different from that of bR, except for the presence of suppressed… CONTINUE READING