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

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Summary

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

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Authors and Affiliations

  1. Cattedra di Chimica e Propedeutica Biochimica, Istituto di Chimica e Chimica Biologica, Ia Facoltà di Medicina e Chirurgia, Università degli Studi di Napoli, Via Constantinopoli 16, I-80138, Napoli, Italy

    E. Bismuto, G. Irace, L. Servillo, A. Giovane & G. Colonna

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  1. E. Bismuto
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  2. G. Irace
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  3. L. Servillo
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  4. A. Giovane
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  5. G. Colonna
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Bismuto, E., Irace, G., Servillo, L. et al. Conformational stability and basal metabolic rate: Reexamination of the case of myoglobin. Experientia 40, 1400–1401 (1984). https://doi.org/10.1007/BF01951911

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  • DOI: https://doi.org/10.1007/BF01951911

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