通过质量光度法揭示的驱动蛋白-链霉亲和素复合物的异质分布。
Heterogeneous distribution of kinesin-streptavidin complexes revealed by mass photometry.
作者信息
Xu Jing, Brown Nathaniel J S, Seol Yeonee, Neuman Keir C
机构信息
Department of Physics, University of California, Merced, CA 95343, USA.
Department of Quantitative and Systems Biology, University of California, Merced, CA 95343, USA.
出版信息
Soft Matter. 2024 Jul 17;20(28):5509-5515. doi: 10.1039/d3sm01702h.
Kinesin-streptavidin complexes are widely used in microtubule-based active-matter studies. The stoichiometry of the complexes is empirically tuned but experimentally challenging to determine. Here, mass photometry measurements reveal heterogenous distributions of kinesin-streptavidin complexes. Our binding model indicates that heterogeneity arises from both the kinesin-streptavidin mixing ratio and the kinesin-biotinylation efficiency.
驱动蛋白-链霉亲和素复合物广泛应用于基于微管的活性物质研究。复合物的化学计量比是根据经验调整的，但通过实验确定具有挑战性。在这里，质量光度测量揭示了驱动蛋白-链霉亲和素复合物的异质分布。我们的结合模型表明，异质性源于驱动蛋白-链霉亲和素的混合比例和驱动蛋白的生物素化效率。
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