Fan Jiang
5 Papers
2 Citations
Fan Jiang is an academic researcher. The author has contributed to research in topics: Chemistry & Medicine. The author has an hindex of 2, co-authored 5 publications.
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Papers
Loosely-packed dynamical structures with partially-melted surface being the key for thermophilic argonaute proteins achieving high DNA-cleavage activity
Lirong Zheng,Huili Lu,Bing Zan,Song-bo Li,Hao Liu,Zhuo Liu,Jian Huang,Yongjia Liu,Fan Jiang,Qian Liu,Yan Feng,Liang Hong +11 more
TL;DR: It is suggested that the highly dynamical structure with a partially-melted surface, distinct from the low-temperature crystalline structure, could be a general strategy assumed by thermophilic pAgos to achieve the high DNA-cleavage activity.
Synthesis of a Near‐Infrared Fluorescence Turn‐On Probe Based on Dicyanoisophorone for HS − ‐Detection in Cancer Cells and Zebrafish in Pure Water Media
TL;DR: In this paper , a dicyanoisophorone-based NIR fluorescent turn-on probe for HS− anions is reported, which displays a highly selective and sensitive (detection limit: 1.35 μM) with emission wavelength at 675 nm in pure water by using a schiff base group as a selective reaction site.
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Enhancement of thermal stability of proteinase K by biocompatible cholinium-based ionic liquids.
TL;DR: It is found that biocompatible cholinium-based ions with appropriately chosen anions can greatly improve the thermal stability of PK, whose melting temperature is increased and the enzymatic activity is slightly reduced in the presence of ILs.
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Mn2+-Induced Structural Flexibility Enhances the Entire Catalytic Cycle and the Cleavage of Mismatches in Prokaryotic Argonaute Proteins
Lirong Zheng,Bing Zan,Bingxin Zhou,Nuolan Li,Banghao Wu,Fan Jiang,Yan Feng,Qian Liu,Liang Hong +8 more
TL;DR: In this article , the unbound Mn2+ significantly enhances the flexibility of diverse pAgo proteins, regardless of their classification as hyperthermophiles, thermophiles or mesophiles.
Creatinase: Using Increased Entropy to Improve the Activity and Thermostability.
Fan Jiang,Jiahao Bian,Hao Liu,Song-bo Li,Xue Bai,Lirong Zheng,Shan Jin,Zhuo Liu,Guangyu Yang,Liang Hong +9 more
TL;DR: In this article , the authors compared the structures, catalytic behaviors, dynamics, and thermostability between a wild-type creatinase and its four-point mutant and found that the mutant is an entropy-driven thermostable protein with higher structural flexibility, i.e., higher conformational entropy in the folded state compared to the wild type.