NMR studies of fluorinated visual pigment analogs.
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.
Department of Chemistry, University of Hawaii, Honolulu 96822.
L U
LU
Colmenares
A E
AE
Asato
M
M
Denny
D
D
Mead
J P
JP
Zingoni
R S
RS
Liu
D005461:Fluorine; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D011487:Protein Conformation; D012243:Rhodopsin / Q000031:analogs & derivatives* / Q000737:chemistry*; D013329:Structure-Activity Relationship
D005461:Fluorine; D012243:Rhodopsin