DICP OpenIR
purificationoftheatgrp7rrmdomainfromarabidopsisthalianaanditspreliminarystructureandbindinganalysis
Chi Xiujuan1; Qiao Xiaoya2; Liu Ying3; Liu Huili4; Chen Lei4; Wang Jihui1; Ai Xuanjun2
Source Publication波谱学杂志
2019-01-01
ISSN1000-4556
Volume36Issue:1Pages:1
AbstractThe glycine-rich RNA-binding protein, AtGrp7, is a component of a negative feedback loop in the circadian clock regulation of Arabidopsis thaliana. In our initial purification trial of the tobacco etch virus (TEV)-cleaved AtGrp7 RNA recognition motif (RRM) domain with the regular protocol, mixed ultraviolet signals of the target proteins and contaminants were observed. A two-step denaturing-refolding protocol was then tested, trying to solve the problem of impurities. The structure of the AtGrp71-90 RRM domain was fully recovered by quick-dilution refolding, evidenced by the fingerprint 1H-15N HSQC spectrum and CS-Rosetta model structures. Isothermal titration calorimetry (ITC) and NMR titration experiments further confirmed that the RRM domain of AtGrp71-90 had proper functions with regards to RNA/DNA binding.
Language英语
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/176757
Collection中国科学院大连化学物理研究所
Affiliation1.大连工业大学
2.中国科学院大连化学物理研究所
3.Division of Virology & Immunology, National Center for AIDS/STD Control and Prevention
4.中国科学院物理研究所
Recommended Citation
GB/T 7714
Chi Xiujuan,Qiao Xiaoya,Liu Ying,et al. purificationoftheatgrp7rrmdomainfromarabidopsisthalianaanditspreliminarystructureandbindinganalysis[J]. 波谱学杂志,2019,36(1):1.
APA Chi Xiujuan.,Qiao Xiaoya.,Liu Ying.,Liu Huili.,Chen Lei.,...&Ai Xuanjun.(2019).purificationoftheatgrp7rrmdomainfromarabidopsisthalianaanditspreliminarystructureandbindinganalysis.波谱学杂志,36(1),1.
MLA Chi Xiujuan,et al."purificationoftheatgrp7rrmdomainfromarabidopsisthalianaanditspreliminarystructureandbindinganalysis".波谱学杂志 36.1(2019):1.
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