Enzymes operating in artificial crowded environments (e.g., polyethylene glycol mimics) exhibit cooperative catalytic dynamics that are spatially entrained by the nanoscale domain organization of biomolecular condensates (e.g., FUS), where local diffusion gradients act as "catalytic hotspots" to restore activity lost under crowding, detectable via single-molecule FRET and enzyme kinetics assays.
Enzymes operating in artificial crowded environments (e.g., polyethylene glycol mimics) exhibit cooperative catalytic dynamics that are spatially entrained by the nanoscale domain organization of biomolecular condensates (e.g., FUS), where local diffusion gradients act as "catalytic hotspots" to restore activity lost under crowding, detectable via single-molecule FRET and enzyme kinetics assays.
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Supporting Research Papers
- Catalytic Crosstalk: Cooperative Enzyme Dynamics in Artificial Crowded Environments
In cellular environments, enzymes operate under densely crowded conditions that often hinder catalytic efficiency by limiting substrate diffusion and essential conformational dynamics. While reports s...
- Enhanced diffusion of colloidal tracers due to enzymatic activity
Enzymatic catalysis can generate nonequilibrium fluctuations, but how these couple to tracer motion at larger length scales depends on physical context. Here, we investigate colloidal tracers in two c...
- Nanoscale domains govern local diffusion and aging within FUS condensates
Biomolecular condensates regulate cellular physiology by sequestering and processing RNAs and proteins, yet how these processes are locally tuned within condensates remains unclear. Moreover, in neuro...
Formal Verification
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