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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Differential chemical and thermal unfolding pattern of Rv3588c and Rv1284 of Mycobacterium tuberculosis - A comparison by fluorescence and circular dichroism spectroscopy.
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Differential chemical and thermal unfolding pattern of Rv3588c and Rv1284 of Mycobacterium tuberculosis - A comparison by fluorescence and circular dichroism spectroscopy.

机译：结核分枝杆菌Rv3588c和Rv1284的化学和热差异展开模式-荧光和圆二色光谱法的比较。

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摘要

The thermal and chemical unfolding pathways of two beta carbonic anhydrases, Rv3588c and Rv1284 of Mycobacterium tuberculosis have been compared by fluorescence and circular dichroism. Chemical and thermal denaturation of the tertiary and secondary structures of these two ubiquitous enzymes of the pathogen reveals that the unfolding of Rv3588c is mediated through the formation of a molten globule intermediate with depleted tertiary structure. However, Rv1284 directly unfolds from the native to the unfolded state. Calculation of the thermodynamic parameters suggest that overall Rv3588c is more stable than Rv1284. Stern-Volmer analysis together with the fluorescence spectra of the proteins suggest that Trp115 in Rv1284 is more buried than Trp10 in Rv3588c. The tryptophan residues in both the proteins are surrounded by positively charged amino acid residues.
机译：通过荧光和圆二色性比较了两种β碳酸酐酶的热和化学解链途径，即结核分枝杆菌的Rv3588c和Rv1284。病原体这两种普遍存在的酶的三级和二级结构的化学和热变性表明，Rv3588c的展开是通过形成三级结构耗尽的熔融小球中间体而介导的。但是，Rv1284从原始状态直接展开到展开状态。热力学参数的计算表明，Rv3588c总体上比Rv1284更稳定。 Stern-Volmer分析以及​​蛋白质的荧光光谱表明，Rv1284中的Trp115比Rv3588c中的Trp10更被掩埋。两种蛋白质中的色氨酸残基被带正电荷的氨基酸残基包围。

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