Abstract
FTIR (Fourier-transform-infrared) difference spectra between cation-free blue and purple bacteriorhodopsin were recorded. The results indicate that during the blue to purple transition no isomerization of the chromophore takes place. It is further observed that approx. 14 water-exposed carboxyl groups ofamino acids are protonated in blue bacteriorhodopsin. The groups were deprotonated during the blue to purple transition. Protonation of carboxyl groups in the interior of the protein, which are not accessible to water, can be excluded.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.