Thermodynamics of 2-Cys Peroxiredoxin Assembly Determined by Isothermal Titration Calorimetry
Barranco-Medina S, Dietz K-J (2009)
In: Biothermodynamics, Part B. Johnson ML, Ackers GK, Holt JM (Eds); Methods in Enzymology, 466. Amsterdam: Elsevier: 409-430.
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Autor*in
Barranco-Medina, Sergio;
Dietz, Karl-JosefUniBi
Herausgeber*in
Johnson, Michael L.;
Ackers, Gary K.;
Holt, Jo M.
Einrichtung
Abstract / Bemerkung
Oligomerization is a frequently encountered physical characteristic of biological molecules that occurs for a wide number of transcription factors, ion channels, oxygen-carrying macromolecules such as hemocyanin and enzymes. On the other hand, unwanted protein oligomerization can lead to the formation of pathogenic structures related with Alzheimer and other diseases. Self-assembly is also a well-described phenomenon within peroxiredoxins, a family of thiol peroxidases. Peroxiredoxin hyperaggregate formation is the key mechanism that triggers the switch between Prx activity as peroxidase and chaperone. The oligomerization process is fundamental for understanding the multiple peroxiredoxin function. The chapter gives a detailed description of typical 2-Cys Peroxiredoxin oligomerization using isothermal titration calorimetry (ITC) and provides a recipe for studying the thermodynamic parameters of peroxiredoxin assembly, that is, association and dissociation constant, enthalpy, entropy, and the Gibbs free energy of the process.
Erscheinungsjahr
2009
Buchtitel
Biothermodynamics, Part B
Serientitel
Methods in Enzymology
Band
466
Seite(n)
409-430
ISBN
978-0-12-374776-1
Page URI
https://pub.uni-bielefeld.de/record/1589290
Zitieren
Barranco-Medina S, Dietz K-J. Thermodynamics of 2-Cys Peroxiredoxin Assembly Determined by Isothermal Titration Calorimetry. In: Johnson ML, Ackers GK, Holt JM, eds. Biothermodynamics, Part B. Methods in Enzymology. Vol 466. Amsterdam: Elsevier; 2009: 409-430.
Barranco-Medina, S., & Dietz, K. - J. (2009). Thermodynamics of 2-Cys Peroxiredoxin Assembly Determined by Isothermal Titration Calorimetry. In M. L. Johnson, G. K. Ackers, & J. M. Holt (Eds.), Methods in Enzymology: Vol. 466. Biothermodynamics, Part B (pp. 409-430). Amsterdam: Elsevier. https://doi.org/10.1016/S0076-6879(09)66017-1
Barranco-Medina, Sergio, and Dietz, Karl-Josef. 2009. “Thermodynamics of 2-Cys Peroxiredoxin Assembly Determined by Isothermal Titration Calorimetry”. In Biothermodynamics, Part B, ed. Michael L. Johnson, Gary K. Ackers, and Jo M. Holt, 466:409-430. Methods in Enzymology. Amsterdam: Elsevier.
Barranco-Medina, S., and Dietz, K. - J. (2009). “Thermodynamics of 2-Cys Peroxiredoxin Assembly Determined by Isothermal Titration Calorimetry” in Biothermodynamics, Part B, Johnson, M. L., Ackers, G. K., and Holt, J. M. eds. Methods in Enzymology, vol. 466, (Amsterdam: Elsevier), 409-430.
Barranco-Medina, S., & Dietz, K.-J., 2009. Thermodynamics of 2-Cys Peroxiredoxin Assembly Determined by Isothermal Titration Calorimetry. In M. L. Johnson, G. K. Ackers, & J. M. Holt, eds. Biothermodynamics, Part B. Methods in Enzymology. no.466 Amsterdam: Elsevier, pp. 409-430.
S. Barranco-Medina and K.-J. Dietz, “Thermodynamics of 2-Cys Peroxiredoxin Assembly Determined by Isothermal Titration Calorimetry”, Biothermodynamics, Part B, M.L. Johnson, G.K. Ackers, and J.M. Holt, eds., Methods in Enzymology, vol. 466, Amsterdam: Elsevier, 2009, pp.409-430.
Barranco-Medina, S., Dietz, K.-J.: Thermodynamics of 2-Cys Peroxiredoxin Assembly Determined by Isothermal Titration Calorimetry. In: Johnson, M.L., Ackers, G.K., and Holt, J.M. (eds.) Biothermodynamics, Part B. Methods in Enzymology. 466, p. 409-430. Elsevier, Amsterdam (2009).
Barranco-Medina, Sergio, and Dietz, Karl-Josef. “Thermodynamics of 2-Cys Peroxiredoxin Assembly Determined by Isothermal Titration Calorimetry”. Biothermodynamics, Part B. Ed. Michael L. Johnson, Gary K. Ackers, and Jo M. Holt. Amsterdam: Elsevier, 2009.Vol. 466. Methods in Enzymology. 409-430.
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