Dr. Wyttenbach received his Ph.D. in 1988 from the University of Basel, Switzerland. After postdoctoral studies at the University of California at Santa Barbara he worked for Bruker-Spectrospin in Switzerland. In 1994 he joined UCSB as a Professional Researcher.
My research efforts with focus on understanding fundamental properties of biological molecules contribute to the research program carried out in the Bowers group. Using methods typically used in the field of Physical Chemistry we examine properties of biomolecules such as their three-dimensional structure (folding), their interaction with solvent molecules, and their propensity to form aggregates. My physical chemistry approach to understanding the complex world of biochemistry is to start with small model systems and progressively increase the complexity of the systems examined. For example, we studied in depth the conformation of small biopolymers (e.g. diglycine through hexaglycine) and in some cases isomerization between different conformers (dinucleotides); we examined systematically various factors contributing to the stability of amino acid zwitterions; and we carefully studied hydration effects by adding individual water molecules to small peptides one by one. Insights gained from these simple systems are essential for attempting to understand results of our projects involving biologically relevant systems such as the hormone oxytocin and proteins involved in misfolding and aggregation phenomena that underlie many diseases including Alzheimer's, Parkinson's, and Mad Cow Disease. As nearly all of the experiments carried out in our group require custom-built instrumentation, I am also interested in instrument design and construction. The machines we build, specially designed mass spectrometers equipped with a drift cell, are used to probe the naked, hydrated, or clustered biomolecules by measuring their masses and/or cross sections at room temperature and often as a function of temperature from 80 K to 600 K. Careful analysis of the experimental results yields, depending on the type of study, information about the molecule shape, about the biomolecule-water interaction, or the extend of biomolecule aggregation. When ever possible, experimental results are compared to theoretical calculations we carry out on large computer systems available to our group. Computations ranging from executing our own code to running standard molecular mechanics/dynamics and high-level ab-initio calculations are designed to theoretically evaluate molecule structures based on their energies and to deduce theoretical values of the experimentally observed quantities (cross sections, water binding energies etc.) for those structures.
Structural Stability from Solution to the Gas Phase: Native Solution Structure of Ubiquitin Survives Analysis in a Solvent-Free Ion Mobility Mass Spectrometry Environment Thomas Wyttenbach and Michael T. Bowers J. Phys. Chem. B 2011, 115, 12266–12275
Ion Mobility-Mass Spectrometry Reveals a Conformational Conversion from Random Assembly to â-Sheet in Amyloid Fibril Formation Christian Bleiholder, Nicholas F. Dupuis, Thomas Wyttenbach, and Michael T. Bowers Nat. Chem. 2011, 3, 172–177
Hydration of Biomolecules Thomas Wyttenbach and Michael T. Bowers Chem. Phys. Lett. 2009, 480, 1-16
Gas-Phase Conformations: The Ion Mobility/Ion Chromatography Method, Thomas Wyttenbach and Michael T. Bowers, Top. Curr. Chem. 2003, 225, 207-232.
Design of a New Electrospray Ion Mobility Mass Spectrometer, Thomas Wyttenbach, Paul R. Kemper, and Michael T. Bowers, Int. J. Mass Spectrom. 2001, 212, 13-23.
On the Stability of Amino Acid Zwitterions in the Gas Phase: The Influence of Derivatization, Proton Affinity, and Alkali Ion Addition, Thomas Wyttenbach, Matthias Witt, and Michael T. Bowers, J. Am. Chem. Soc. 2000, 122, 3458-3464.