【摘 要】
：
DsbC, a disulfide isomerase with chaperone activity in the periplasm, is a homodimeric protein, while the activity of DsbC monomer has not been known so far
【机 构】
：
Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences and National La
【出 处】
：
第二届全国“跨学科蛋白质研究”学术讨论会
论文部分内容阅读
DsbC, a disulfide isomerase with chaperone activity in the periplasm, is a homodimeric protein, while the activity of DsbC monomer has not been known so far.Here we report how the heat triggered oxidative activity of DsbC monomer was uncovered from our T-jump time-resolved IR spectroscopic study.Determined by using temperature-dependent Fourier transform infrared and time-resolved infrared spectroscopy coupled with temperature jump initiation, thermally induced unfolding of DsbC exhibited a three-state transition with midpoint temperature of 35.7℃ and 74.5℃, respectively.In contrast, the unfolding of G49R, a monomeric mutant, showed only a two-state transition with 83.3℃ as the midpoint, which corresponds to the second transition assigned to the global unfolding and aggregation of the subunits in the unfolding of DsbC.
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