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First ASMS Hites Award for Outstanding Research Publication Presented to Prof. Alison Ashcroft for Her Use of Waters Synapt HDMS System to Explore Protein Complexes
Date:6/3/2009

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 Seat
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