A5087853330- Supramolecular Self-Assembly in Materials
- Glycosylation and Glycoproteins Research
- Monoclonal and Polyclonal Antibodies Research
- Protein Structure and Dynamics
- Enzyme Structure and Function
- Advanced Biosensing Techniques and Applications
- Bacteriophages and microbial interactions
- Advanced biosensing and bioanalysis techniques
- Hemoglobin structure and function
- Crystallography and molecular interactions
- Hydrogels: synthesis, properties, applications
- Diatoms and Algae Research
- RNA and protein synthesis mechanisms
- Connective tissue disorders research
- Nanoparticle-Based Drug Delivery
- Chemical Synthesis and Analysis
- Supramolecular Chemistry and Complexes
Fudan University
2017-2024
Abstract In nature, proteins self‐assemble into various structures with different dimensions. To construct these nanostructures in laboratories, normally symmetries are selected. However, most of approaches engineering‐intensive and highly dependent on the accuracy protein design. Herein, we report that a simple native LecA assembles one‐dimensional nanoribbons nanowires, two‐dimensional nanosheets, three‐dimensional layered controlled mainly by small‐molecule assembly‐inducing ligands RnG (...
Abstract Red fluorescent proteins (RFPs) are powerful tools used in molecular biology research. Although RFP can be easily monitored vivo, manipulation of by suitable nanobodies binding to different epitopes is still desired. Thus, it crucial obtain structural information on how the interact with RFP. Here, we determined crystal structures LaM2‐mCherry and LaM4‐mCherry complexes at 1.4 1.9 Å resolution. Our results showed that LaM2 binds side mCherry β‐barrel, while LaM4 bottom β‐barrel. The...
We introduced a small molecular "inducing ligand" strategy to crystallize proteins via dual noncovalent interactions. Here we demonstrate that the variant protein-packing frameworks of concanavalin A (ConA) binding with ligands are controlled by different crystallization methods. Besides, protein crystalline also small-molecule inducing RnM (n = 1–5), which varies in number ethylene oxide repeating units. To better understand mechanism packing ligands, all-atom dynamic (MD) simulations were...
Abstract In nature, proteins self‐assemble into various structures with different dimensions. To construct these nanostructures in laboratories, normally symmetries are selected. However, most of approaches engineering‐intensive and highly dependent on the accuracy protein design. Herein, we report that a simple native LecA assembles one‐dimensional nanoribbons nanowires, two‐dimensional nanosheets, three‐dimensional layered controlled mainly by small‐molecule assembly‐inducing ligands RnG (...
Biomolecules may undergo dynamic transitions between different aggregation states in order to adapt the microenvironment. As a result, appropriate biofunctions can be performed only under certain states. This feature inspires exploration for constructing and regulating environmentally adaptive materials through supramolecular ways. Herein, we propose strategy employ special pair of interactions, very strong binding fluorescent proteins their nanobodies together with rather weak...
In this study, a new mechanism on CO<sub>2</sub>-responsiveness of protein microtubules constructed by dual non-covalent interactions has been demonstrated.
In der Natur …… bilden Proteine hochgeordnete selbstorganisierte Strukturen mit einer Vielzahl an Morphologien und Dimensionen. Zuschrift auf S. 10831 ff. berichten Y. Ma, G. Chen et al. über die Erzeugung von Proteinaggregaten dem nativen Protein LecA als Baustein, indem sie Zucker-Protein-Wechselwirkungen Rhodamindimerisierung nutzten. Die Dimensionen Proteinaggregate lassen sich Länge Verknüpfung Zucker Rhodamin einstellen.
Abstract Background Red fluorescent proteins (RFPs) are widely used in molecular biology research, especially deep tissues and animal models, because of their superior autofluorescence, light scattering, phototoxicity to GFP. Although RFP can be easily monitored vivo , improved manipulation is still desired. Using suitable nanobodies (Nbs) bind different epitopes the most promising approach; thus, it crucial obtain structural information on how Nbs interact with RFP. Results We determined...
Abstract Red fluorescent proteins (RFPs) are widely used in molecular biology research, especially deep tissues and animal models, because of their superior autofluorescence, light scattering, phototoxicity to GFP. Although RFP can be easily monitored vivo , improved manipulation is still desired. Using suitable nanobodies (Nbs) bind different epitopes the most promising approach; thus, it crucial obtain structural information on how Nbs interact with RFP. We determined crystal structures...