ASMS judged the publication on the basis of its "innovative aspects, technical quality, likely stimulation of future research, likely impact on future applications, and the quality of the presentation."
Prof. Ashcroft received the Award and $2,000 cash stipend at a ceremony on Wednesday, June 3, in Philadelphia at the 57th ASMS Conference on Mass Spectrometry and Allied Topics.
The Award is named in honor of Professor Ronald A. Hites of Indiana University who spearheaded the creation of JASMS in 1988 while President of ASMS. JASMS is devoted to the publication of research papers covering all aspects of mass spectrometry from all fields of science including chemistry, physics, geology, environmental, biological, health and life sciences.
Prof. Ashcroft's laboratory was one of the first scientific laboratories to acquire a Waters SYNAPT(TM) HDMS System to study the function of protein molecules and their assembly into macromolecular complexes. Proteins are carefully folded, three-dimensional long-chain molecules assembled by the human body. When properly folded they regulate normal bodily functions. Several high profile diseases including Alzheimer's, Creuzfeldt-Jakob's, and Parkinson's, can develop when certain proteins become misfolded, causing a chain of events that can lead to self-aggregation and amyloid fibril formation. Thus determining a protein's folded state is important and mass spectrometry is unique in its ability to monitor independently co-populated biomolecules in heterogeneous ensembles. Other research from this Group is directed at unraveling the mechanism of virus capsid assembly and determining the sub-unit specificity of pilus assembly.
Shortly after purchasing her SYNAPT(TM) HDMS System in 2007, Prof. Ashcroft had this to say about it. "It's adding a new dimension to our research. We can now quantify the amount of protein that is in its native state and the amount that is unfolded and partially folded. We can also monitor which particular conformers are consumed during the assembly process. This is providing important new insights and detail into how biomolecules work at the molecular level," adds Prof. Ashcroft.
The full reference for Prof. Ashcroft's article in the Journal of the American Society of Mass Spectrometry is:
Monitoring co-populated conformational states during protein folding events using ESI-IMS-MS, D. P. Smith, K. Giles, R. H. Bateman, S. E. Radford, A. E Ashcroft, J. Am. Soc. Mass Spectrom., 2007 Dec; 18 (12): 2180 - 90, DOI:10.1016/j.jasms.2007.09.017
Waters introduced the SYNAPT HDMS System at the American Society of Mass Spectrometry annual meeting in Seattle in June of 2006. It is the first commercially-available mass spectrometer with the ability to analyze ions by their size, shape and charge in addition to mass.
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