Conformational stability and basal metabolic rate: Reexamination of the case of myoglobin
- 1 December 1984
- journal article
- research article
- Published by Springer Nature in Cellular and Molecular Life Sciences
- Vol. 40 (12) , 1400-1401
- https://doi.org/10.1007/bf01951911
Abstract
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 isolatedKeywords
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