F
Fang Tian
Researcher at Nanjing University
Publications - 15
Citations - 390
Fang Tian is an academic researcher from Nanjing University. The author has contributed to research in topics: Chemistry & Force spectroscopy. The author has an hindex of 5, co-authored 10 publications receiving 96 citations.
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Journal ArticleDOI
N501Y mutation of spike protein in SARS-CoV-2 strengthens its binding to receptor ACE2.
Fang Tian,Bei Tong,Liang Sun,Shengchao Shi,Bin Zheng,Zibin Wang,Xianchi Dong,Xianchi Dong,Peng Zheng +8 more
TL;DR: In this paper, the authors used a cell surface-binding assay, a kinetics study, a single-molecule technique, and a computational method to investigate the interaction between these RBD (mutations) and ACE2.
Posted ContentDOI
Mutation N501Y in RBD of Spike Protein Strengthens the Interaction between COVID-19 and its Receptor ACE2
TL;DR: Wang et al. as discussed by the authors combined cell surface binding assay, kinetics study, single-molecule technique, and computational method to investigate the interaction between these RBD (mutations) and ACE2.
Journal ArticleDOI
Combination of Click Chemistry and Enzymatic Ligation for Stable and Efficient Protein Immobilization for Single-Molecule Force Spectroscopy
TL;DR: Protein immobilization is an essential method for both basic and applied research into protein, and the covalent, site-specific attachment is the most desirable strategy.
Journal ArticleDOI
Verification of sortase for protein conjugation by single-molecule force spectroscopy and molecular dynamics simulations.
TL;DR: The use of sortase for protein conjugation is verified, and a longer linker with a higher glycine content should be used with caution, because of the high probability of a closed conformation.
Journal ArticleDOI
Single-Molecule Force Spectroscopy Reveals that the Fe-N Bond Enables Multiple Rupture Pathways of the 2Fe2S Cluster in a MitoNEET Monomer.
Guobin Song,Xuan Ding,Huaxing Liu,Guodong Yuan,Fang Tian,Shengchao Shi,Yang Yang,Guoqiang Li,Peng Zheng +8 more
TL;DR: This work used atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS) to investigate the mechanical unfolding mechanism of an mNT monomer and found that the Fe-N bond was the weakest point of the cluster, the rupture of which occurred first, and could be independent of the clusters break.