Waters has announced that the American Society for Mass Spectrometry (ASMS) has presented Prof Alison Ashcroft of the University of Leeds with the Ron Hites Award.
The award was made for Outstanding Research Publication in the Journal of the American Society of Mass Spectrometry (JASMS).
Ashcroft's paper, titled 'Monitoring Co-populated Conformational States during Protein Folding Events Using Electrospray Ionisation-Ion Mobility Spectrometry-Mass Spectrometry', appeared in the December 2007 issue of JASMS.
It was co-authored by Waters scientists Kevin Giles and Robert Bateman along with University of Leeds researchers David Smith and Professor Sheena Radford.
Ashcroft's team acquired the research data for the publication on a Waters Synapt high-definition MS (HDMS) system.
Ashcroft is manager of the mass spectrometry facility in the Astbury Centre for structural molecular biology at the University of Leeds.
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'.
Ashcroft received the award and USD2,000 cash stipend at a ceremony on 3 June, in Philadelphia at the 57th ASMS Conference on Mass Spectrometry and Allied Topics.
The award is named in honour 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.
Ashcroft's laboratory was one of the first scientific laboratories to acquire a Waters Synapt 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.
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 unravelling the mechanism of virus capsid assembly and determining the sub-unit specificity of pilus assembly.