DENVER – At a ceremony held today during the 59th annual meeting of the American Society for Mass Spectrometry (ASMS), University of Michigan Dept. of Chemistry Assistant Professor Brandon Ruotolo received an ASMS 2011 Research Award in recognition of his accomplishments with mass spectrometry. This year marks the 25th year of Waters’ sponsorship of the award.

In presenting the award to Dr. Ruotolo, Waters’ Lance Nicolaysen, Ph.D. said, “We couldn’t be more pleased with the selection of Dr. Ruotolo as this year’s recipient of the Waters Research Award. As pioneers in discovery, Dr. Ruotolo and his team deserve credit for the taking on the task of uncovering the many unknowns around disease causation, progression, and treatment. We wish Dr. Ruotolo and his team continued success.”

Recipients of the Waters Research Award are selected by an independent panel of mass spectrometry scientists and experts. The year 2011 marks 25 consecutive years of Waters award sponsorship. The award is being presented to the University of Michigan in the name of Dr. Ruotolo.

Dr. Ruotolo’s research team is developing new approaches and methods based primarily upon ion mobility-mass spectrometry, aimed at determining which large multi-protein complexes are responsible for causing or contributing to amyloid/protein aggregation diseases such Alzheimer’s, diabetes type II, ALS and cancer- related multi-protein systems involved in DNA replication.

Since joining the University of Michigan faculty Dr. Ruotolo has been the recipient of several NIH research grants totaling more than $2 million. He was also the recipient of the 2011 Ralph E. Powe Junior Faculty Enhancement Award granted by the Oak Ridge Associated Universities to recognize and assist outstanding junior faculty.

In a statement, Dr. Ruotolo laid out the challenges his team is aiming to overcome during the course of their research:

“Within each living organism proteins are at work acting as the molecular machines that preside over every aspect of cellular function from synthesis to programmed cell death. A key factor in protein functionality is their ability to self-assemble and interact with one another to create vast molecular ‘machines’ or complexes, capable of recruiting non-protein agents (i.e., DNA) and performing intricate cellular tasks. Such complexes are often transient in nature, continually associating and dissociating. Further complicating matters, many of these essential multi-protein machines are present within minute quantities within each cell. This situation frames one of the great challenges for the field of structural biology: to understand the structure and function of the cellular protein machine inventory – particularly those dynamic protein machines present in very low numbers within a massive background of other macromolecules that make up cells.”

Prior to his faculty appointment to the University of Michigan in 2009, Dr. Ruotolo worked as a research fellow under Prof. Carol Robinson at the University of Cambridge, Cambridge, England. Two years ago, Dr. Ruotolo sat down with Waters to discuss his research. In this interview, Dr. Ruotolo details the challenges he faces as a research scientist on the front lines of scientific discovery.

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SOURCE: Waters Corporation