The key to the function (or malfunction) of a protein is closely linked to its three-dimensional shape.  Ion mobility mass spectrometry, as a tool for probing molecular shape, has the potential to play an important role in the study of proteins.  Over the years, mass spectrometry has proven to be a valuable tool in understanding intrinsic chemical properties.  With the emergence in the past decade of new ionization methods, mass spectrometry can now be extended as a tool to study biomolecules on a fundamental level.  Our experimental and theoretical methods allow us to investigate structure, aggregation and energetics in a variety of protein systems.  In addition, we are able to explore correlations between solution- and gas-phase protein structures.  We are currently investigating proteins involved in several different neurological diseases.  Alzheimer’s disease, Parkinson’s disease and transmissible spongiform encephalopathies (TSEs) all involve protein misfolding and subsequent aggregation in the brain.  The proteins associated with each disease are listed below.  The conformational and aggregation aspects involved in these systems make them ideally suited for study using ion mobility mass spectrometry.


  1. "Amyloid β-protein monomer structure: A computational and experimental study" A. Baumketner, S. L. Bernstein, T. Wyttenbach, G. Bitan, D. B. Teplow, M. T. Bowers, J.-E. Shea Protein Sci., in press

  2. "Amyloid β-protein: Monomer structure and early aggregation states of Aβ42 and its Pro19 alloform" S. L. Bernstein, T. Wyttenbach, A. Baumketner, J.-E. Shea, G. Bitan, D. B. Teplow, M. T. Bowers J. Am. Chem. Soc. 2005, 127, 2075-2084

  3. "α-Synuclein: Stable compact and extended monomeric structures and pH dependence of dimer formation" S. L. Bernstein, D. Liu, T. Wyttenbach, M. T. Bowers, J. C. Lee, H. B. Gray, J. R. Winkler J. Am. Soc. Mass Spectrom. 2004, 15, 1435-1443