The Center (MSC-AMHERST) provides state-of-the-art analytical equipment, analytical services and expertise in mass spectrometry for UMass-Amherst, neighboring scientific communities, researchers from other institutions and industries. Currently, MSC-AMHERST serves the needs of more than 30 groups with active life science research interests by facilitating a) development of novel polymers and other organic/inorganic synthetic materials; b) identification and quantitation of metabolites; c) analysis of variety of post-translational modifications in proteins, including biopharmaceuticals; d) quantitative comparative analysis of protein levels; e) fundamental studies in protein/protein and protein/ligand interaction research areas etc., owing to its expanding capabilities in modern methods of mass spectrometry.
MSC-AMHERST is also actively used within the framework of the NIH-funded Chemistry-Biology Interface (CBI) program (5T32 GM008515-15). Nineteen training faculty of the CBI program are users of the Facility’s instrumentation.
MSC-AMHERST houses a wide range of mass spectrometry and chromatography instruments, including Hybrid Quadrupole Time-of-Flight (Applied Biosystems QStar-XL), Double-Focusing Magnetic Sector (JEOL-700 MStation), Fourier-Transform Ion-Cyclotron Resonance (Bruker's SolariX 7T FT-ICR), Thermo Orbitrap Fusion, Waters Synapt G2 Si with HDX Automation, Waters Xevo TQD Triple QuadrupoleMatrix-Assisted Laser Desorption Ionization (MALDI-MicroFlex), Bruker Esquire-LC Ion Trap and MicrOTOF-II mass-spectrometers, several HPLC, UPLC and GC systems.
Representative publications supported by MSC-AMHERST
- 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