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Updated: Aug 21, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Structural and functional changes of bovine carbonic anhydrase as a consequence of temperature
N S Sarraf1, A A Saboury, B Ranjbar
1Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.
Abstract:
The temperature dependence of the activity and structure of the enzyme carbonic anhydrase was studied. The Arrhenius plot shows a jump which is seen usually in proteins with more than one subunit or with one subunit but more than one domain. Since carbonic anhydrase has only one subunit with one domain, the fine conformational changes of the protein motifs could only be detected through circular dichroism polarimetry. It seems that the jump in Arrhenius plot is a result of some slight structural changes in the secondary and tertiary structures of the enzyme.
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