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NMR studies of fluorinated visual pigment analogs
L U Colmenares1, A E Asato, M Denny
1Department of Chemistry, University of Hawaii, Honolulu 96822.
Biochemical and Biophysical Research Communications
|September 30, 1991
Abstract:
The 19F-nmr chemical shift data of isomeric pigments (11-cis and 9-cis) of four vinyl fluororhodopsins and two trifluororhodopsins have been recorded. When compared with model protonated Schiff bases, a set of F-nmr opsin shift parameter (FOS) was obtained. The data revealed regiospecific protein perturbations on the F-resonances. They can be interpreted in terms of specific protein interactions such as the postulated second point charge and other polar interactions as well as the common hydrophobic protein perturbation.