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科学家以原子级别的分辨率拍摄正在展开的蛋白质

“Snapshot” of the unfolding of the CylR2 protein from Enterococcus faecalis. If the protein is cooled from 25°C to -16°C, it successively breaks down into its two identical subunits. The latter are initially stable, but at -16°C they form an instable, dynamic protein form, which plays a key role in folding. (Image: Zweckstetter, Max Planck Institute for Biophysical Chemistry & German Center for Neurodegenerative Diseases)

现在,研究人员首次“拍摄”到一种蛋白质如何逐渐展开。

通过将低温与核磁共振分光法相结合,科学家在将CylR2蛋白质从25摄氏度冷却到16摄氏度的同时对它的七个中间形式进行了视觉化。他们的研究结果显示,最不稳定的中间形式对于蛋白质的折叠起重要作用。

科学家的发现可能有助于更好地理解蛋白质如何形成其所具有的结构以及在疾病中如何发生错误的折叠。

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Cold denaturation of a protein dimer monitored at atomic resolution

Nature Chemical Biology, 10 February 2013 | doi:10.1038/nchembio.1181

Protein folding and unfolding are crucial for a range of biological phenomena and human diseases. Defining the structural properties of the involved transient species is therefore of prime interest. Using a combination of cold denaturation with NMR spectroscopy, we reveal detailed insight into the unfolding of the homodimeric repressor protein CylR2. Seven three-dimensional structures of CylR2at temperatures from 25 °C to −16 °C reveal a progressive dissociation of the dimeric protein into a native-like monomeric intermediate followed by transition into a highly dynamic, partially folded state. The core of the partially folded state seems critical for biological function and misfolding.

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