Scientists improved enzyme-based biosensors by modifying MOFs to enhance electron transfer and enzyme stability. Enzymes are ...
Researchers at University of Tsukuba have developed a new material that harnesses the power of enzymes more effectively.
Each enzyme molecule has a special place called the active site where another molecule, called the substrate, fits. The substrate goes through a chemical reaction and changes into a new molecule ...
Enzymes are able to bind to their substrate because they have an active site. An induced fit occurs where the active site of the enzyme is changed slightly to better fit the substrate after the ...
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Improving the performance of biosensors: New material effectively harnesses the power of enzymesThe modified material acts as a "wire," allowing efficient electron exchange between the enzyme and electrode. Furthermore, the design of the MOFs allows easy access to the buried active sites of ...
(Image: National Human Genome Research Institute) Enzymes are highly specific to their substrates, the molecules upon which they act. The active site of an enzyme has a unique three-dimensional ...
Enzymes are also involved in the building up of chemical molecules elsewhere in the body. In an organism, the active site of each enzyme is a different shape. It is a perfect match to the shape of ...
These programs were instrumental to our project because they allowed us to do 'structural studies' and whittle down which ...
Since enzymes are quite efficient biocatalysts active under mild conditions, they are expected to be applied to varieties of environmentally benign chemical processes realized in the next generation.
The structural analysis of redox enzymes in their reduced and oxidized states is crucial for advancing bioelectronic devices like biosensors and biofuel cells. In a recent study, researchers from ...
The modified material acts as a "wire," allowing efficient electron exchange between the enzyme and electrode. Furthermore, the design of the MOFs allows easy access to the buried active sites of ...
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