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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >How the dyes affect folding of small proteins in single-molecule FRET experiments: A simulation study
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How the dyes affect folding of small proteins in single-molecule FRET experiments: A simulation study

机译：染料如何影响单分子FRET实验中的小蛋白质的折叠：模拟研究

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摘要

A key question in the application of the single-molecule F?rster resonance energy transfer (smFRET) technique to study protein folding is how the dyes affect the protein behavior. Understanding of these effects is particularly important for small proteins, for which the dyes, along with their linkers, can be comparable in size (mass) with the protein. Using a coarse-grained model, we simulated folding of BBL protein and two of its FRET constructs. The obtained results suggest that even for small proteins, such as the 45-residue BBL, the appearance of the excluded volume in the protein conformation space due to the presence of dyes does not change the overall picture of folding. At the same time, some deviations from folding of the original protein are observed, in particular, the FRET constructs fold considerably slower than the original protein because the protein collapse in the initial state of folding is slowed down due to the protein loading with relatively massive dyes.
机译：在施用单分子f？rste共振能量转移（SMFRet）技术的关键问题是研究蛋白质折叠的是染料如何影响蛋白质行为。 对这些效果的理解对于小蛋白质尤其重要，其中染料以及它们的接头，可以与蛋白质的大小（质量）相当。 使用粗粒模型，我们模拟了BBL蛋白的折叠和其两个褶皱构建体。 所得结果表明，即使对于小蛋白质，例如45-残基BBL，由于染料的存在而导致的蛋白质构象空间中排除体积的外观不会改变折叠的整体图像。 同时，观察到原始蛋白质的折叠的一些偏差，特别是褶皱构造比原始蛋白质相当慢，因为由于蛋白质负载具有相对较大的蛋白质载荷，初始折叠状态下的蛋白质塌陷减慢 染料。

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