Stephen Eyles

Extension Associate Professor

Our goal in the Mass Spectrometry Center is to engage researchers and provides state of the art analytical instrumentation, analytical services and expertise in mass spectrometry for UMass Amherst, neighboring scientific communities and their collaborators. The Center currently serves the needs of more than 50 research groups with active life science research interests, ranging from confirmation of organic synthesis products and synthetic polymer studies, to analysis of modifications in proteins and macromolecular complexes, as well as protein folding, assembly and dynamics investigated through chemical labeling and cross linking. Staff can provide instrument training to students and researchers, as well as expert advice on experimental design and data interpretation. Life science focused research in the Center includes projects to identify and quantify proteins in complex matrices as well as metabolites. The goal is to provide expertise, training and instrumental assistance to researchers so that they can optimize usage of the equipment and maximize the utility of data obtained.

Current Research
Protein dynamics is critical to understanding the processes involved in protein homeostasis, for example the mechanisms of chaperone action to maintain healthy folded proteins, or the mechanisms of protein oligomerization leading to aggregation or formation of amyloid plaques. Current research interests include applying mass spectrometry methodologies to investigate protein-protein interactions, through hydrogen-deuterium exchange and chemical cross linking, as well as using hydrogen exchange to study protein folding and dynamics. The multitude of uses for mass spectrometry in the biophysical arena is rapidly evolving, and IALS at UMass Amherst is at the forefront of this technology, developing new techniques to study the fate of proteins and other biomolecules in and out of the cell. The Mass Spectrometry Center makes leading edge technology available to researchers in order to address these critically important questions. See the MS Center website for further details about instrumentation available.

Learn more at www.umass.edu/massspec

Academic Background

BA University of Oxford, UK, 1986
DPhil University of Oxford, UK, 1990
Postdoctoral Training: University of Massachusetts Amherst

Selected Publications

Guerra, D., Truebridge, I., Eyles, S.J., Treffon, P., Vierling, E. (2018) “Direct measurement of S-nitrosothiols with an Orbitrap Fusion mass spectrometer: S-nitrosoglutathione reductase as a model protein” Methods Molec. Biol., 1747, 143-160.

He, T., Gershenson, A., Eyles, S.J., Lee, Y.J., Liu, W.R., Wang, J., Roberts, M.F. (2015) “Fluorinated aromatic amino acids distinguish cation- interactions from membrane insertion” J. Biol. Chem. 290, 19334-19442.

Koshy, S.S., Eyles, S.J., Weis, R.M., Thompson, L.K., Kaltashov, I.A., Eyles, S.J. Hydrogen exchange mass spectrometry of functional membrane-bound chemotaxis receptor complexes. Biochemistry (2013) 52, 8833-8842.

http://massspec.biochem.umass.edu/

Koshy, S.S., Li, X., Eyles. S.J., Weis, R.M., Thompson, L.K. (2014) “Hydrogen exchange differences between chemoreceptor signaling complexes localize to functionally important subdomains” Biochemistry 53, 7755-7764.

Mass Spectrometry in Structural Biology and Biophysics: Architecture, Dynamics and Interaction of Biomolecules, 2nd edition, John Wiley & Sons. 2012. 325 pp.

http://massspec.biochem.umass.edu/

Al-Amier, H., Eyles, S.J., Craker, L.E. Evaluation of extraction methods for isolation and detection of formononetin in black cohosh (Actaea racemosa L.). J. Medicinally Active Plants (2012) 1, 6-12.

http://massspec.biochem.umass.edu/

Eyles, S.J., Gierasch, L.M. Nature's molecular sponges: Small heat shock proteins grow into their chaperone roles. Proc. Natl. Acad. Sci. (2010) 107, 2727-2728.

http://massspec.biochem.umass.edu/

Kaltashov, I.A., Abzalimov, R.R., Eyles, S.J., Frimpong, A.K. (2008) “Studies of intact proteins and protein complexes: ESI MS approaches” In: Mass Spectrometry Analysis for Protein-Protein Interactions and Dynamics. M. Chance, ed. Boston: Wiley-Blackwell, 2008. pp. 215-240.

http://massspec.biochem.umass.edu/

Stephen Eyles

Institute for Applied Life Sciences