Dr. John Engen is not one to shy away from a challenge. As he is quick to point out, “We don’t work on the proteins in HIV and cancer because they are easy. The experiments we perform are complex and challenging. But we work on these proteins because if we can learn something about them, perhaps we can do something about the diseases related to them.”
A pioneer in the combined use of hydrogen-deuterium exchange (H/DX) technology, UPLC® and ion mobility mass spectrometry, Dr. Engen is a leading expert on understanding proteins and protein confirmation, more specifically on how chemically active sites on a protein structure are affected by conformation and the impact that this might have on disease.
He is the recipient of numerous scientific honors, including the Arthur F. Findeis Award, Division of Analytical Chemistry, American Chemical Society (2009), the Barnett Institute Innovative Research Award (2006), and the Sigma Xi Young Investigator Award, New Mexico Chapter (2005).
Technology, key to the complex work he performs, includes Waters SYNAPT® time-of-flight MS systems coupled with Waters UPLC separation systems as well as specialized data management software co-developed with Waters.
But with a scientist like Prof. Engen, sometimes even the most advanced is not advanced enough.
His experimental protocols benefit from fast, low temperature separation of complex peptide mixtures; however high quality separations are difficult under these conditions.
So Prof. Engen turned to the minds who had always served him so well, the scientists at Waters. Prof. Engen and a Waters team collaborated on the development of a custom LC instrument. The result is an instrument for the laboratory now known as the nanoACQUITY UPLC® System with HDX Technology.
Results have been beyond expectation--- the best chromatography either group had ever seen for this application. Working faster and easier than ever before, this unique partnership has led to early successes and will hopefully lead to more effective therapies for those suffering from disease.
“With the custom instrument we made with Waters, we can work on things never dreamed possible a year earlier,” says Engen. “Now we’re working with proteins that are ten times the size of what we worked with before. In a couple of years, I think we’ll laugh and say now we work with proteins that are fifty times that size! It’s possible because the technology keeps getting better and better.”
The only commercially-available complete system for HXMS studies.
November 2, 2011
Studying the structure of antibodies that neutralize HIV function with the help of H/D exchange mass spectrometry.