Stephen Eyles

Stephen Eyles, PhD

Institute for Applied Life Sciences
S503 Life Sciences Laboratories
240 Thatcher Road
Amherst, MA 01003

(413) 577-1528
eyles@umass.edu
Mass Spectrometry Core Facility

Director of Mass Spectrometry, Director of Biophysical Characterization

Extension Associate Professor of Biochemistry and Molecular Biology

Steve has been Director of the Mass Spectrometry Core Facility at UMass Amherst since 2000. He has been involved in mass spectrometry and other biophysical and analytical techniques since grad school, working on developing novel methodologies to study biomolecular structure and dynamics. He has co-authored a book on Mass Spectrometry in Biophysics. Steve holds an undergraduate degree and D.Phil. in Chemistry from the University of Oxford.

Our goal in the Mass Spectrometry Core Facility is to engage researchers and provide state of the art analytical instrumentation, analytical services, and expertise in mass spectrometry for UMass Amherst, neighboring scientific communities, and their collaborators. The Core currently serves the needs of more than 50 research groups across campus 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-ligand and protein-protein interactions as well as protein dynamics, through the use of hydrogen-deuterium exchange and chemical cross-linking. 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 Core Facility makes leading-edge technology available to researchers in order to address these critically important questions. See the MS Core website for further details about instrumentation available.

Learn more at Mass Spectrometry Core Facility

Academic Background

BA/MA University of Oxford, UK, 1990
DPhil University of Oxford, UK, 1995
Postdoctoral Training: University of Massachusetts Amherst

Associated Facility / Faculty / Staff
  • Mass Spectrometry

    Expertise measuring molecular weights of small molecules, biological and synthetic macromolecules, qualitative and quantitative proteomics, protein dynamics.

    • Core Facilities Staff 
    • Center for Bioactive Delivery 
    • Models to Medicine Center 
    • Protein Homeostasis