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• W2023343036 abstract "Abstract Despite the growing structural information on receptors and G proteins, the information on affinities and kinetics of protein-protein and protein-nucleotide interactions is still not complete. In this study on photoactivated rhodopsin (R*) and the rod G protein, Gt, we have used kinetic light scattering, backed by direct biochemical assays, to follow G protein activation. Our protocol includes the following: (i) to measure initial rates on the background of rapid depletion of the GtGDP substrate; (ii) to titrate GtGDP, GTP, and GDP; and (iii) to apply a double displacement reaction scheme to describe the results. All data are simultaneously fitted by one and the same set of parameters. We obtain values of K m = 2200 Gt/μm2 for GtGDP andK m = 230 μm for GTP; dissociation constants are K d = 530 Gt/μm2 for R*-GtGDP dissociation and K d = 270 μm for GDP release from R*GtGDP, once formed. Maximal catalytic rates per photoexcited rhodopsin are 600 Gt/s at 22 °C and 1300 Gt/s at 34 °C. The analysis provides a tool to allocate and quantify better the effects of chemical or mutational protein modifications to individual steps in signal transduction." @default.
• W2023343036 created "2016-06-24" @default.
• W2023343036 creator A5021314496 @default.
• W2023343036 creator A5064368106 @default.
• W2023343036 date "2001-03-01" @default.
• W2023343036 modified "2023-10-13" @default.
• W2023343036 title "Maximal Rate and Nucleotide Dependence of Rhodopsin-catalyzed Transducin Activation" @default.
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• W2023343036 doi "https://doi.org/10.1074/jbc.m009475200" @default.
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• W2023343036 hasPublicationYear "2001" @default.
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