, Volume 40, Issue 12, pp 1400–1401 | Cite as

Conformational stability and basal metabolic rate: Reexamination of the case of myoglobin

  • E. Bismuto
  • G. Irace
  • L. Servillo
  • A. Giovane
  • G. Colonna
Short Communications


The free energy of unfolding of several myoglobins from different animal species has been determined from their denatunation pattern by using the ligand binding model. The results indicate that no simple correlation exists between the free energy of unfolding of myoglobin and the basal metabolic rate of the animal species from which the myoglobin was isolated

Key words

Myoglobin conformational stability basal metabolic rate unfolding, free energy of 


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Copyright information

© Birkhäuser Verlag 1984

Authors and Affiliations

  • E. Bismuto
    • 1
  • G. Irace
    • 1
  • L. Servillo
    • 1
  • A. Giovane
    • 1
  • G. Colonna
    • 1
  1. 1.Cattedra di Chimica e Propedeutica Biochimica, Istituto di Chimica e Chimica Biologica, Ia Facoltà di Medicina e ChirurgiaUniversità degli Studi di NapoliNapoli(Italy)

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