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

accumulate in the joints of dialysis patients and which are associated with dialysis-related amyloidosis. A detailed understanding of these processes at the molecular level will aid in the design of therapeutics.

New Form of Mass Spectrometry Giving New Dimensions to Biological Research

As a tool, conventional mass spectrometry is an excellent method for differentiating between proteins having different masses. However, as different conformers, or folded forms, of a particular protein have identical masses, it is virtually impossible to differentiate them by conventional means. That's where the Waters SYNAPT HDMS System, and its embedded ion mobility technology, has helped the University of Leeds.

"A protein can fold into a very compact 3-D structure or under certain conditions it can unfold into a more expanded structure. Even though these different 3-D structures have the same mass and mass-to-charge (m/z) ratio, the ion mobility capability of the SYNAPT HDMS System can separate them and tell you how much of the protein is in its folded form vs. the unfolded form. And as the cross-sectional areas of the two protein conformers are different, by being able to separate them by shape, the SYNAPT HDMS System allows us to distinguish between the various protein forms. The results are really amazing," says Dr. Alison Ashcroft, Reader in Biomolecular Mass Spectrometry and Mass Spectrometry Facility Manager.

The SYNAPT System from Waters has provided the lab with new insights into the assembly process. "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 Dr. Ashcroft.

Waters introduced the SYNAPT HDMS System at the American Soci
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SOURCE Waters Corporation
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