Abstract
Proteins from psychrophilic organisms can function at low temperatures and have shown potential for industrial applications. In the present study, thermal denaturation of a psychrophilic adenylate kinase (AKpsychro) from Bacillus globisporus was measured using circular dichroism spectroscopy and its molecular dynamics (MD) simulations were performed. The results from the unfolding experiment and MD simulations of AKpsychro were compared with those of its mesophilic and thermophilic homologues to study the relationship between dynamic motion and the cold adaptation of proteins.
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More From: Journal of the Korean Society for Applied Biological Chemistry
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