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.
Every enzyme has a place in which the molecule fits exactly. This is known as the active site. The active site of the catalase allows the hydrogen peroxide molecule to fit exactly. You could say ...
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 ...
These programs were instrumental to our project because they allowed us to do 'structural studies' and whittle down which ...
They proposed a Cu(II)-bound OCR as a key intermediate for the hydrogen atom abstraction (HAA), which behaves like an active site of a copper-based enzyme both structurally and functionally.
IIT Roorkee researchers use esterase enzyme to break down carcinogenic plasticizers, paving the way for a plastic-free future.
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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