Low thermodynamic but high kinetic stability of an antifreeze protein from Rhagium mordax.


The equilibrium heat stability and the kinetic heat tolerance of a recombinant antifreeze protein (AFP) from the beetle Rhagium mordax (RmAFP1) are studied through differential scanning calorimetry and circular dichroism spectroscopy. In contrast to other insect AFPs studied with this respect, the RmAFP1 has only one disulfide bridge. The melting… (More)
DOI: 10.1002/pro.2459


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