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首页> 外文期刊>Journal of Molecular Biology >A Similar In Vitro and In Cell Lysate Folding Intermediate for the FF Domain
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A Similar In Vitro and In Cell Lysate Folding Intermediate for the FF Domain

机译：用于FF结构域的体外和细胞裂解物折叠中间体相似

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摘要

Understanding the mechanisms by which proteins fold into their three-dimensional structures, including a description of the intermediates that are formed during the folding process, remains a goal of protein science. Most studies are performed under carefully controlled conditions in which the folding reaction is monitored in a buffer solution that is far from the natural milieu of the cell. Here, we have used ~(13)C and ~1H relaxation dispersion NMR spectroscopy to study folding of the FF domain in both Escherichia coli and Saccharomyces cerevisiae cellular lysates. We find that a conformationally excited state is populated in both lysates, which is very similar in structure to a folding intermediate observed in previous studies in buffer, with the kinetics and thermodynamics of the interconversion between native and intermediate conformers somewhat changed. The results point to the importance of extending folding studies beyond the test tube yet emphasize that insights can be obtained through careful experiments recorded in controlled buffer solutions.
机译：理解蛋白质折叠成其三维结构的机制，包括在折叠过程中形成的中间体的描述，仍然是蛋白质科学的目标。大多数研究是在小心控制的条件下进行，其中在远离细胞的天然Milieu的缓冲溶液中监测折叠反应。在这里，我们已经使用〜（13）C和〜1H弛豫分散性NMR光谱，以研究大肠杆菌和酿酒酵母细胞裂解物中FF结构域的折叠。我们发现构象激发的状态在两个裂解物中填充，其结构非常相似，在缓冲液中的先前研究中观察到的折叠中间体，其中天然和中间符合材料之间的互连的动力学和热力学稍微改变。结果指出了在试管超出试管超出折叠研究的重要性，但强调可以通过在受控缓冲溶液中记录的仔细实验获得洞察。

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