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KMID : 0613820040140020309
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Journal of Life Science
2004 Volume.14 No. 2 p.309 ~ p.314
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Application of Temperature Gradient Gel Electrophoresis To cAMP Receptor Protein
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Gang Jong-Back
Cho Hyun-Young
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Abstract
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Cyclic AMP receptor protein (CRP) is involved in the transcriptional regulation of more than 100 genes in E. coli. CRP dimer is converted into active form via the sequential conformation change of cAMP binding pocket, hinge region and HTH DNA binding motif by binding of cAMP. The temperature gradient gel electrophoresis (TGGE) was applied to CRP protein to know whether it was an efficient technique to study the conformational transitions and the thermal stability. TGGE showed the unfolding process of wild-type and S83G CRP proteins with the temperature gradient set from 29 to 71℃ on nondenaturing polyacrylamide gel. Melting temperature (Tm) was 57±1 and 55±1℃ for wild-type and S83G CRP, respectively in acidic buffer[89.8 mM Glycine and 24 mM Boric acid (pH 5.8)].
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KEYWORD
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Cyclic AMP receptor protein, Protease digestion, Tm (melting temperature), Protein denaturation
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