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Disruption of a potential disulfide bond of Cys65-Cys141 on the structure and stability of globin X from zebrafish

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成果类型:
期刊论文
作者:
Pan, Aiqun;Liu, Xichun*;Han, Hui;Gao, Shu-Qin;Lin, Ying-Wu
通讯作者:
Liu, Xichun;Lin, YW
作者机构:
[Han, Hui; Pan, Aiqun; Lin, Ying-Wu; Liu, Xichun; Liu, XC] Univ South China, Sch Chem & Chem Engn, Hengyang 421001, Peoples R China.
[Gao, Shu-Qin; Lin, Ying-Wu] Univ South China, Lab Prot Struct & Funct, Hengyang 421001, Peoples R China.
通讯机构:
[Lin, YW ; Liu, XC] U
Univ South China, Sch Chem & Chem Engn, Hengyang 421001, Peoples R China.
Univ South China, Lab Prot Struct & Funct, Hengyang 421001, Peoples R China.
语种:
英文
期刊:
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
ISSN:
1463-9076
年:
2025
卷:
27
期:
5
页码:
2828-2833
基金类别:
National Natural Science Foundation of China [32171270, 22107046]; National Natural Science Foundation of China; CAS (Hefei, China)
机构署名:
本校为第一且通讯机构
院系归属:
化学化工学院
摘要:
Globin X is a newly discovered member of the globin family, while its structure and function are not fully understood. In this study, we performed protein modelling studies using Alphafold3 and molecular dynamics simulations, which suggested that the protein adopts a typical globin fold, with the formation of a potential disulfide bond of Cys65 and Cys141. To elucidate the role of this unique disulfide in protein structure and stability, we constructed a double mutant of C65S/C141S by mutating the two cysteine residues to serine. As suggested by protein mass, ultraviolet-visible (UV-Vis) and c...

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