Add Yahoo as a preferred source to see more of our stories on Google. Chemists have long dreamed of mimicking nature’s precision, and now, thanks to a repurposed enzyme, they’ve taken a leap closer.

For the first time, researchers have succeeded in predicting how to change the optimum temperature of an enzyme using large computer calculations. A cold-adapted enzyme from an Antarctic bacterium was ...

The molecular structure of an enzyme from a marine bacterium with potential industrial uses has been determined by RIKEN ...

We therefore long suspected that the crucial cyclization reaction could occur spontaneously, without the help of another enzyme," says Sarah O'Connor, explaining the starting point of the research.

Unhackneyed compartmentalization generated by audible sound allows the enzyme reactions to be controlled spatiotemporally. Spatiotemporal regulation of multistep enzyme reactions through ...

It is well known in physics and chemistry that equal charges repel each other, while opposite charges attract. It was long assumed that this principle also applies when enzymes – the biological ...

CHAPEL HILL – All biological reactions within human cells depend on enzymes. Their power as catalysts enables biological reactions to occur usually in milliseconds. But how slowly would these ...

For the first time, researchers have successfully used computational simulations to modify an enzyme’s structure to increase the optimum temperature of a reaction. Researchers at Uppsala University ...

Researchers from the University of Liverpool, Japan, and Argentina have captured atomic-resolution images of an important ...

Takeaki Ozawa and his team from the University of Tokyo reveal the metabolic reactions upon activating an enzyme called Akt2. In doing so, they reveal the inner workings of insulin-regulated ...