相关实验视频

Updated: Jun 5, 2025

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
12:07

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET

Published on: October 9, 2021

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附录A2野生型与E53A,E96A,D162A,E247A和D322A突变体的结构特征,物理化学特性和结合能力的差异

Sunisa Yoodee1, Sirikanya Plumworasawat1, Thanyalak Malaitad1

  • 1Medical Proteomics Unit, Research Department, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok, 10700, Thailand.

Archives of biochemistry and biophysics
|December 14, 2024
PubMed
概括

这项研究通过突变其结域来研究Annexin A2 (ANXA2). 关键突变显著改变了ANXA2的结构,特性和结合能力,特别是E96A和D322A.

关键词:
附录A2 附录A2 附录A2结合性亲缘关系是一种结合性亲缘关系.生物信息学是一种生物信息学.静电电静电学 静电电静电学水性 水性 水性一个单点突变突变.局部导向的突变发生.

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