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Updated: Jun 4, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
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Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

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对交叉链接器骨干结构对蛋白质动态分析影响的全面调查:Pin1的案例研究

Zichun Qiao1, Min Sun2, Zhou Gong3

  • 1State Key Laboratory of Medical Proteomics, CAS Key Laboratory of Separation Science for Analytical Chemistry, National Chromatographic R. & A. Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, Liaoning, 116023, China; University of Chinese Academy of Sciences, Beijing, 100049, China.

Talanta
|December 30, 2024
PubMed
概括

交叉连接器的骨干结构显著影响蛋白质动态形状分析. 乙烯基甘醇 (BS(PEG) 2) 提供了对NIMA相互作用的Peptidyl-prolyl cis-trans异构酶1 (Pin1) 动态的卓越洞察力.

关键词:
交叉连接器的骨干结构结构.交叉连接质谱法 交叉连接质谱法乙基-乙基 cis-trans 异构酶 NIMA-交互作用的 1 (Pin1)蛋白质的动态构造结构.

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