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

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2015-12
2016-02

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2016-02

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

Published Date

2020-04-17

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Experimental Data
Observational Data

Abstract

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-C

Description

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.

Referenced by

Olivieri, C., Wang, Y., Li, G. C., Subrahmanian, M. V., Kim, J., Stultz, B. R., ... & Gao, J. (2020). Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A. Elife, 9, e55607.
https://doi.org/10.7554/eLife.55607

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NIH GM 100310 to G.V

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Suggested citation

Li, Geoffrey; Muretta, Joseph; Olivieri, Cristina. (2020). Analysis of the kinetics of binding of Protein Kinase A Inhibitor alpha (PKIa) to cAMP-dependent protein kinase a catalytic subunit (PKA-C). Retrieved from the Data Repository for the University of Minnesota (DRUM), 10.13020/jxk9-x251.

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