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Thermal Inactivation and Unfolding of a Dimeric Arginine Kinase

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Thermal inactivation and unfolding of the dimeric arginine kinase (AK) from sea cucumber Stichopus japonicus was investigated. The activation energy was calculated to be 388 kJ/mol. Based on the analysis of the denaturation course at 58°C, a model is suggested for the thermal unfolding of this dimeric AK. In addition, the effect of free Mg2+ and the potential biological significance on the thermal unfolding of dimeric AK is discussed.

Keywords: arginine kinase; differential scanning calorimetry; fast performance liquid chromatography; fluorescence; inactivation; mg; thermal denaturation; unfolding

Document Type: Review Article


Affiliations: Department of Biological Science and Biotechnology, School of Life Sciences and Engineering, Tsinghua University, Beijing 100084 China.

Publication date: May 1, 2005

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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