Isothermal Titration Calorimetry to Study Plant Peptide Ligand-Receptor Interactions
© 2024. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature..
The field of plant receptor biology has rapidly expanded in the past three decades. However, the demonstration of direct interaction between receptor-ligand pairs remains a challenge. Identifying and quantifying protein-ligand interactions is crucial for understanding how they regulate certain physiological processes. An important aspect is the quantification of different parameters of the interaction, like binding affinity, kinetics, and ligand specificity that drive the formation of signaling complexes. In this chapter, we discuss Isothermal Titration Calorimetry (ITC) as a label-free technique to measure thermodynamic parameters of ligand binding with high accuracy and reproducibility. We provide a detailed guideline how to design, perform, analyze, and interpret ITC measurements using as an example the interaction between the SCHENGEN3/GASSHO1 (SGN3/GSO1) leucine-rich repeat receptor-like kinase and its sulfated peptide ligand CASPARIAN STRIP INTEGRITY FACTOR 2 (CIF2).
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 2023 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:2731 |
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| Enthalten in: |
Methods in molecular biology (Clifton, N.J.) - 2731(2023) vom: 29., Seite 295-310 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Lanooij, Judith [VerfasserIn] |
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| Links: |
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| Themen: |
Binding affinity |
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| Anmerkungen: |
Date Completed 30.11.2023 Date Revised 30.11.2023 published: Print Citation Status MEDLINE |
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| doi: |
10.1007/978-1-0716-3511-7_22 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 520 | |a The field of plant receptor biology has rapidly expanded in the past three decades. However, the demonstration of direct interaction between receptor-ligand pairs remains a challenge. Identifying and quantifying protein-ligand interactions is crucial for understanding how they regulate certain physiological processes. An important aspect is the quantification of different parameters of the interaction, like binding affinity, kinetics, and ligand specificity that drive the formation of signaling complexes. In this chapter, we discuss Isothermal Titration Calorimetry (ITC) as a label-free technique to measure thermodynamic parameters of ligand binding with high accuracy and reproducibility. We provide a detailed guideline how to design, perform, analyze, and interpret ITC measurements using as an example the interaction between the SCHENGEN3/GASSHO1 (SGN3/GSO1) leucine-rich repeat receptor-like kinase and its sulfated peptide ligand CASPARIAN STRIP INTEGRITY FACTOR 2 (CIF2) | ||
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