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In the Forefront of Research into Protein Folding and Macromolecular Complex Assembly
Date:12/4/2007

University of Leeds Publishes Results Acquired With Waters SYNAPT High

Definition MS System

MILFORD, Mass. and LEEDS, England, Dec. 4 /PRNewswire-FirstCall/ -- Waters Corporation (NYSE: WAT) announced today that the University of Leeds' Astbury Centre for Structural Molecular Biology has published the results of protein research conducted with its newly-acquired Waters(R) SYNAPT High Definition MS(TM) (HDMS) System in the Journal of the American Society of Mass Spectrometry (JASMS).

The SYNAPT(R) HDMS System is being used by the Ashcroft Laboratory to study the function of biological molecules. In an article appearing in the December 2007 issue of the JASMS, researchers at Leeds describe the successful separation and analysis of various folded forms of the proteins cytochrome c and beta-2-microglobulin, an achievement the Ashcroft Laboratory hopes will lead to a more complete understanding of the biological processes responsible for amyloid fibril formation, bacterial pilus aggregation and virus capsid assembly -- all associated with debilitating diseases.

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 normally folded into a particular shape become misfolded, causing a chain of events that can lead to self-aggregation and amyloid fibril formation. Dr. Alison Ashcroft and her colleague Prof. Sheena Radford at the University of Leeds are studying one such protein, beta-2-microglobulin, to try to understand how it forms such fibrils which
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