Researchers at Stanford University have developed a tool that is claimed to significantly speed up the study of enzymes. The tool enables scientists to run very small experiments simultaneously using one polymer chip. The tool has been specifically developed to allow researchers to study enzymes faster and more efficiently compared to conventional methods.
Enzymes are protein molecules that pack amino acids to catalyze the conversion of one type of molecule into another. They enable reactions within the body such as digestion, fermentation, and others. Without enzymes, these processes would be extremely slow.
Years of research in months
Researchers say a chemical reaction that would take longer than the lifespan of the universe can happen in seconds with the aid of enzymes. Since enzymes are so useful, a lot of research has been carried out for them. We know their structure and the chemical groups they use for reactions. However, details of how enzymes connect to the functions and how they perform biochemical transitions at such speeds are yet to be known.
The new tool is called HT-MEK, which stands for High-Throughput Microfluidic Enzyme Kinetics. The tool ensures to cut short years of research into just a few weeks by running thousands of enzyme experiments simultaneously. Study co-leader Dan Herschlag suggested that limits in performing enough experiments have restricted science from understanding enzymes.
New tool revealing new details
The new tool could reveal clues about how distant parts of enzymes come together to perform a specific task by enabling scientists to deeply probe beyond the small “active site” of an enzyme where binding happens.
HT-MEK makes use of two existing technologies to make analysis faster, including microfluidics and cell-free protein synthesis. The device is automated that enables researchers to use printers to deposit microscopic spots of synthetic DNA coding for the enzyme they want to observe. The scientists used the new tech on a well-studied enzyme called PafA and discovered mutations beyond the active site affected its ability to start chemical reactions.
