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NMR studies of protein folding and binding in cells and cell-like environments

机译:核磁共振研究蛋白质在细胞和类细胞环境中的折叠和结合

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摘要

Proteins function in cells where the concentration of macromolecules can exceed 300 g/L. The ways in which this crowded environment affects the physical properties of proteins remain poorly understood. We summarize recent NMR-based studies of protein folding and binding conducted in cells and in vitro under crowded conditions. Many of the observations can be understood in terms of interactions between proteins and the rest of the intracellular environment (i.e. quinary interactions). Nevertheless, NMR studies of folding and binding in cells and cell-like environments remain in their infancy. The frontier involves investigations of larger proteins and further efforts in higher eukaryotic cells.
机译:蛋白质在大分子浓度可能超过300 g / L的细胞中起作用。这种拥挤的环境影响蛋白质物理特性的方式仍然知之甚少。我们总结了最近在细胞和体外在拥挤条件下进行的蛋白质折叠和结合的基于NMR的研究。可以从蛋白质与其余细胞内环境之间的相互作用(即三元相互作用)来理解许多观察结果。然而,在细胞和类细胞环境中进行折叠和结合的NMR研究仍处于初期阶段。前沿领域涉及对更大蛋白质的研究以及对更高等真核细胞的进一步努力。

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