RNA Chaperones pp 137-150 | Cite as

Kinetic and Thermodynamic Analyses of RNA–Protein Interactions

  • Ryo Amano
  • Taiichi SakamotoEmail author
Part of the Methods in Molecular Biology book series (MIMB, volume 2106)


Recently created biophysical methods, such as surface plasmon resonance (SPR) and isothermal titration calorimetry (ITC), have been widely used to quantitatively study biomolecule interactions. The dissociation constant of the interaction with kinetic parameters, such as association rate constant and dissociation rate constant, can be obtained using SPR analysis. With thermodynamic parameters, such as enthalpy change and entropy change, the dissociation constant can be obtained by ITC analysis. Both methods differ not only in the type of information obtained but also in throughput and sample concentration. Analyzing the biophysical parameters of RNA–protein interactions will help us understand their functions in biological processes. In this chapter, we describe step-by-step SPR and ITC protocols suitable to study the kinetics and thermodynamics of RNA–protein interactions.

Key words

RNA Protein Dissociation constant Enthalpy Entropy 



This study was supported by JSPS KAKENHI Grant Number JP15K06982, JP18K11536 from The Ministry of Education, Sports, Culture, Science and Technology (MEXT) of Japan.


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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2020

Authors and Affiliations

  1. 1.The Institute of Medical Science, Project Division of RNA Medical ScienceThe University of TokyoTokyoJapan
  2. 2.Department of Life Science, Faculty of Advanced EngineeringChiba Institute of TechnologyChibaJapan

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