Abstract
Cyclic AMP receptor proteins(CRP) activate many genes in Escherichia coli by binding of cAMP with not fully known mechanism. CRP existed as apo-CRP in the absence of cAMP, <TEX>$CRP;(cAMP)_2$</TEX><TEX>$_2$</TEX> at low(micromolar) cAMP concentration, or <TEX>$CRP;(cAMP)_4$</TEX> at high(millimolar) concentration of cAMP. This study is designed to measure the thermal stability of S83G CRP, which substituted glycine for serine at amino acid 83 position, with CD spectrapolarimeter at 222nm by the constant elevation of temperature from <TEX>$20^{\circ]C\; to\; 90^{\circ}C\; at\; 1^{\circ}C/min$</TEX>. The non-linear regression analysis showed that melting temperatures were 68.4, 72.0, and <TEX>$82.3^{\circ}C$</TEX> for no cAMP, 0.1mM cAMP, and 5mM cAMP, respectively. Result showed the strong thermal stability of CRP by binding of additional cAMP molecules to region between the hinge region and helix-turn-helix(HTH) motif at 5mM cAMP concentration.
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