Abstract
The thermal denaturation of adenosine deaminase has been investigated in the presence and absence of dodecyl trimethyl ammonium bromide (DTAB) over the temperature range (305-355 K) in 2.5 m M phosphate buffer, pH 6.4 by temperature scanning spectroscopy. The presence of DTAB caused the destabilization of adenosine deaminase resulting in a decrease in the temperature of unfolding with increase in DTAB concentration. The temperature dependence of the spectroscopic behavior of the enzyme at 280 nm was interpreted in terms of the two-state model of protein unfolding and used to determine thermodynamic parameters for the unfolding process.
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