多聚酸性氨基酸对蛋白质性质的影响

doi:10.3969/j.issn.2095-1736.2023.01.021

Journal of Biology ›› 2023, Vol. 40 ›› Issue (1): 21-.doi: 10.3969/j.issn.2095-1736.2023.01.021

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Poly acidic amino acids sequence drives variation of protein in hydrodynamic properties

LI Yafei^1,2,3,4, WU Shenyang^1,2,3,4, CHU Wendan^1,2,3,4, ZHOU Cuiyan^1,2,3,4,SHI Qinghua⁵, LI Wenqi^1,2,3,4

1. Institute of Biomedicine, Tsinghua University, Beijing 100084, China; 2. National Protein Science Facility,
Beijing 100084, China; 3. School of Life Sciences, Tsinghua University, Beijing 100084, China;
4. Beijing Advanced Innovation Center for Structural Biology, Tsinghua University, Beijing 100084, China;
5. International School of Beijing, Beijing 101300, China

Online:2023-02-18 Published:2023-02-21

Abstract

Abstract: 选取碳末端富含酸性氨基酸的拟南芥 SnRK2.6(sucrose non-fermenting1-related protein kinase 2.6)和人源PDI(protein disulfide isomerase)，以及近球形蛋白拟南芥 PYL10 (PYR like protein 10)，分别将重复酸性氨基酸序列添加到SnRK2.6(1-332)、PDI(1-440)、PYL10碳末端，利用大肠杆菌BL21重组表达，经过亲和层析，离子交换层析和分子排阻层析进行纯化，综合利用分析超速离心技术，分子排阻层析技术以及多角度静态光散射技术，研究人为设计的多聚氨基酸末端对蛋白质分子排阻行为，聚合状态和其他水力学性质的影响。结果发现，多聚酸性氨基酸末端虽不影响蛋白质分子的聚合状态，但会明显减少分子排阻色谱中蛋白质的洗脱体积，影响蛋白质分子的斯托克斯半径和轴长比等水力学性质。

Key words: analytical ultracentrifugation, static light scattering, size exclusion chromatography, poly acidic amino acids sequence, hydrodynamic property

CLC Number:

LI Yafei, WU Shenyang, CHU Wendan, ZHOU Cuiyan, SHI Qinghua, LI Wenqi. Poly acidic amino acids sequence drives variation of protein in hydrodynamic properties[J]. Journal of Biology, 2023, 40(1): 21-.

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Poly acidic amino acids sequence drives variation of protein in hydrodynamic properties

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