Enthalpy-entropy compensation phenomena in serine (Pro) enzyme: Inhibitor complex formation

G. Amiconi, P. Ascenzi, M. Bolognese, M. Guarneri, E. Menegatti

Research output: Contribution to journalArticle

Abstract

Thermodynamics concerning the interaction of the bovine basic pancreatic trypsin inhibitor as well as bovine and porcine pancreatic secretory trypsin inhibitor with some serine (pro)enzymes has been obtained at pH 8.0 (I = 0.1 M) between 5 °C and 45 °C. Results have been analyzed by the enthalpy-entropy compensation plot (ΔHo ° versus ΔSo) and linear relationships obtained, suggesting the involvment of protein conformation and possibly hydration in the process(es) of protein-protein interaction(s).

Original languageEnglish
Pages (from-to)177-180
Number of pages4
JournalAdvances in the Biosciences
Volume65
Issue numberC
Publication statusPublished - 1987

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Keywords

  • (pro)enzyme:inhibitor complexes
  • enthalpy-entropy compensation phenomena
  • macromolecular inhibitors
  • Serine (pro)enzymes
  • thermodynamics

Cite this

Amiconi, G., Ascenzi, P., Bolognese, M., Guarneri, M., & Menegatti, E. (1987). Enthalpy-entropy compensation phenomena in serine (Pro) enzyme: Inhibitor complex formation. Advances in the Biosciences, 65(C), 177-180.