Tamura A, Kojima S, Miura K, Sturtevant J M
Department of Chemistry, Yale University, New Haven, Connecticut 06520.
Biochemistry. 1994 Dec 6;33(48):14512-20. doi: 10.1021/bi00252a018.
The effect of an engineered disulfide bond between two identical subunits of a dimeric protein, Streptomyces subtilisin inhibitor, on the stability of the protein was studied by differential scanning calorimetry. The introduction of the linkage caused a large stabilization without changing the cooperativity of unfolding, with the denaturation temperature of a 2 mg/mL solution being increased by 14.3 degrees C to 95.0 degrees C at pH 9.5 and by 16.4 degrees C to 63.0 degrees C at pH 3.0. The stabilization was caused by a loss of denaturational entropy, i.e., -40 and -98 cal K-1 mol-1 at pH 3.0 and 9.5, respectively, which more than compensated for the loss in the denaturational enthalpy.
通过差示扫描量热法研究了二聚体蛋白质枯草芽孢杆菌蛋白酶抑制剂两个相同亚基之间的工程二硫键对蛋白质稳定性的影响。引入该连接导致了显著的稳定作用，而不改变解折叠的协同性，在pH 9.5时，2 mg/mL溶液的变性温度升高了14.3℃至95.0℃，在pH 3.0时升高了16.4℃至63.0℃。这种稳定作用是由变性熵的损失引起的，即在pH 3.0和9.5时分别为-40和-98 cal K-1 mol-1，这足以弥补变性焓的损失。
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