Analysis of the kinetics of binding of Protein Kinase A Inhibitor alpha (PKIa) to cAMP-dependent protein kinase a catalytic subunit (PKA-C)

Abstract

In the excel file are summarized the TR-FRET raw data used for the analysis of the binding kinetic for PKIa to ATP-saturated PKA-C. All the experiments were acquired at Biophysical Technology Center (BMBB Department, University of Minnesota, Minneapolis, MN) by GL and JM within The analysis of the TR-FRET data was performed by GL and JM.TR-FRET raw data used for the analysis of the binding kinetic for full-length protein kinase inhibitor (PKIa) to ATP-saturated cAMP-dependent protein kinase A (PKA-C). The experiments are part of a publication on eLIFE: "Multi-state Recognition Pathway of the Intrinsically Disordered Protein Kinase Inhibitor by Protein Kinase A", where we investigated the structural and kinetics changed that PKIa undergoes upon interaction with PKA-CNIH GM 100310 to G.