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.
Colmenares
L U
LU
Department of Chemistry, University of Hawaii, Honolulu 96822.
Asato
A E
AE
Denny
M
M
Mead
D
D
Zingoni
J P
JP
Liu
R S
RS
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