The mystery of the electron microscope
By John Walker The electron microscope has never been as good at revealing the inner workings of molecules as it is now.
But this has been because its primary function has always been to look for patterns and details in molecules.
The latest example of this is the study of the valence electrons of proteins, which have been used to measure the atomic weights of proteins.
But scientists have been searching for other ways of looking at valence particles to understand how proteins interact with their environment.
In a paper published this week in the journal Science, a team of researchers led by the University of Washington says they have developed a novel method for detecting and measuring the valences of proteins in a new electron microscope.
The method uses a small number of highly sensitive sensors to detect electrons that are produced by the binding of an amino acid with a carbon atom.
“This technique is very sensitive to the amount of electrons,” says graduate student James D. Schilling.
“It’s much more sensitive than a standard electron microscope.”
The researchers say their new technique, which was developed by the UW’s Materials Science and Engineering Department, is a very promising alternative to conventional methods of electron microscopy.
In fact, the new technique could make it easier to use electron microscopes in a wide variety of labs, says the study’s senior author, graduate student Jennifer E. Filippo.
She has worked with the UW team to design and test their new system.
The new method, she says, is particularly useful in the study and measurement of proteins that are involved in a large number of different processes, such as the production of amino acids and the synthesis of proteins for human health and medicine.
“What this technique can do is it’s really good at measuring the structure and the structure of the proteins and the chemical interactions between them,” she says.
This is a great result, says Schilling, because “it means we can actually measure and quantify the structure, and that means we’re able to quantify the chemical interaction between the protein and its environment.”
The new system, known as the ion-beam ion chromatography-electrospray tandem mass spectrometer (IBED-ESM), is based on a type of electron microscope that can only measure the valentines and nines of a molecule, but it can also measure the chemical composition of the molecule.
The researchers use the technique to measure, for example, how many electrons are produced from the binding with the amino acid to the carbon atom of a specific amino acid.
The team then measures the electron counts of these valentine-nine pairs with an electron microscope and with an ion-exchange laser.
This results in a spectra that the team then compares with those of the original spectra.
They then use this comparison to estimate the total number of electrons produced by a protein to determine its overall chemical composition.
“We can also use these to look at the chemical structure of individual molecules and tell us how that affects the overall structure of a protein,” Schilling says.
The UW researchers’ approach is based, in part, on the fact that protein molecules contain an abundance of an abundant number of valentates and ninos, or pairs of these two atoms.
“The fact that we can measure and analyze the chemical compositions of individual protein molecules and the amount and type of valence is an exciting thing,” Schills says.
“Because it tells us how important the valents are in the structure.”
In addition to protein, the team also studied a number of other proteins that have been known to interact with molecules, including a group of enzymes called the glycolytic enzymes, which break down proteins and then use the carbon atoms to form the amino acids that the enzymes need.
“So these proteins have been studied for a long time,” Schiller says.
However, because they are also involved in so many other processes, the UW researchers say, their approach is particularly important for proteins that may be involved in cell growth and metabolism, as well as in many other functions.
The scientists used a variety of different proteins in their study.
The study found that the valency electrons were produced primarily by a group called a glycoglycylase.
These glycoolytic enzymes help to break down complex sugars and amino acids, and are important in the process of producing the essential amino acids needed by many other life processes, including growth, development, and repair of cells.
“They are actually the most important ones to look out for,” Schill says.
But they are not the only ones.
“There are many other glyco glycylases that can be used,” he says.
Schill and Filippos hope that their new method can help scientists understand how the glycolipase, a member of the glycosyltransferase family of enzymes, works and how it is used in a number, if not all, of the other enzymes involved in the degradation of proteins and other molecules.
“Our work provides a new way to measure