The Mass Spectrometry Center at UMass Amherst maintains a suite of state-of-the-art analytical mass spectrometry equipment, providing analytical services and expertise in mass spectrometry to researchers across a broad range of disciplines at UMass-Amherst and neighboring academic institutions, as well as in collaboration with industrial partners. Mass spectrometry services facilitate a range of research in the life sciences, as well as in chemistry and polymer science. Examples include characterization of intact proteins, determining sites of chemical or post-translational modification using top-down and bottom-up approaches, metabolite and other natural product determination and quantitation, as well as analysis of novel synthetic organic/inorganic compounds and polymeric materials. Other research groups who make use of the Center instrumentation are involved in investigation of protein dynamics by hydrogen/deuterium exchange, understanding and tailoring enzyme mechanisms, and also MS method development and fundamental studies in protein/protein and protein/ligand interaction.
Instrumentation in the Mass Spectrometry Center is incorporated into various academic courses at the undergraduate and graduate level, including interdisciplinary programs such as the Chemistry-Biology interface link, Institute for Cellular Engineering link. Recent funding from the Commonwealth of Massachusetts to create the Institute for Applied Life Sciences (link) has enabled substantial improvements in the capabilities of the Center, particularly with regard to the burgeoning field of biological mass spectrometry.
Instrumentation in the Center encompasses a broad range of analytical capabilities from small molecule analysis to large biopolymers, including GC-MS, HPLC-MS, UPLC and nanoLC chromatography systems. For more details, see Instrumentation.
Representative publications supported by the Mass Spectrometry Center
- Hangasky JA., Saban E., Knapp MJ. (2013) Inverse solvent isotope effects arising from substrate triggering in the factor inhibiting hypoxia inducible factor Biochemistry. 52(9), 1594-1602 link
- Abzalimov RR., Bobst CE., Kaltashov IA. (2013) A new approach to measuring protein backbone protection with high spatial resolution using H/D exchange and electron capture dissociation Anal Chem. 85(19), 9173-9180 link
- Pektas, Knapp MJ. (2013) Substrate preference of the HIF-prolyl hydroxylase-2 (PHD2) and substrate-induced conformational change J Inorg Biochem. 126, 55-60 link
- Abzalimov RR., Bobst CE, Salinas PA, Savickas P, Thomas JJ, Kaltashov IA (2013) Studies of pH-Dependent self-association of a recombinant form of arylsulfatase A with electrospray ionization mass spectrometry Anal Chem. 85(3), 1591-1596 link
- Kaltashov, I.A., Eyles, S.J. (2012) Mass Spectrometry in Structural Biology and Biophysics: Architecture, Dynamics and Interaction of Biomolecules, 2nd edition, John Wiley & Sons, 289 pp. (ISBN: 978-0-470-93779-2) link
- Al-Amier, H., Eyles, S.J., Craker, L.E. (2012) “Evaluation of extraction methods for isolation and detection of formononetin in black cohosh (Actaea racemosa L.)” J. Medicin. Active Plants, 1, 6-12. link
- R.R. Abzalimov, Frimpong A.K., Kaltashov I.A. (2012) Detection and characterization of large-scale protein conformational transitions in solution using charge-state distribution analysis in ESI-MS Methods. Mol. Biol. 896, 365-373 link
- R.R. Abzalimov, Frimpong A.K., Kaltashov I.A. (2012) Structural characterization of protein-polymer conjugates. I. Assessing heterogeneity of a small PEGylated protein and mapping conjugation sites using ion exchange chromatography and top-down tandem mass spectrometry Int. J. Mass Spectrom. 312, 135-143 link
- Velazquez-Delgado, E. M. and Hardy J.A. (2012) “Phosphorylation regulates assembly of the caspase-6 substrate-binding groove.” Structure 20, 742-751 link
- G. Wang, R.R. Abzalimov, I.A. Kaltashov (2011) Direct Monitoring of Heat-Stressed Biopolymers with Temperature-Controlled Electrospray Ionization Mass Spectrometry Anal Chem. 83(8), 2870-2876 link
- Eyles, S.J., Gierasch, L.M. (2010) Nature's molecular sponges: Small heat shock proteins grow into their chaperone roles Proc. Natl. Acad. Sci. 107, 2727-2728 link