Evaluation of the Kinetic and Transient Phase Thermodynamic Parameters for the Refolding of Staphylococcal Nuclease by pH-Jump Method.

概要

論文の詳細を見る
Refolding process of Staphylococcal nuclease was observed by the pH-jump stopped-flow method using fluorescence intensity increase of the protein as a probe. The refolding of the protein by the pH-jump from 1.6 to 6.7 was tri-phasic, and the values of three apparent rate constants, k1, k2, and k3 were evaluated to be 9.5, 1.0, and 0.03s-1, respectively (25°C). The transient phase-thermodynamic parameters were evaluated from the temperature dependence of the kinetic constants. Small activation enthalpy and large entropy change accompanied the k1-phase. The values k1 and k2 decreased remarkably at acidic region but k3 did not, the results indicating that the k1- and k2-phases reflect deprotonation processes.
日本熱測定学会の論文