Olivieri, CristinaVeglia, Gianluigi2022-01-032022-01-032022-01-03https://hdl.handle.net/11299/225840Raw and processed (GraphPad format) for the kinetics of binding between immobilized human PKA-C and RKIPwt obtained by biolayer interferometry analysis (BLItz - ForteBio). NMR chemical perturbation (CSP) analysis of the amide chemical shift of RKIPwt and P74L RKIP mutant in complex with ATPγN-saturatedPKA-C and CSP analysis of the amide chemical shifts of human PKA-C in complex with RKIP, under ATPγN saturating condiction.Kinetical and structural characterization of the interaction between the RAF kinase inhibitor (RKIP) and the cAMP-dependent protein kinase A (PKA-C) by interferometry and nuclear magnetic resonance (NMR) spectroscopy analysis. Together with the analysis performed by Dr. Marsha Rosner's laboratory (University of Chicago), these studies are part of a paper that has been sent to the PNAS journal.CC0 1.0 Universalhttp://creativecommons.org/publicdomain/zero/1.0/Protein kinase ARaf kinase inhibitor RKIPChemical shiftInterferometry analysisNMRDatasethttps://doi.org/10.13020/39bz-0r13