Nuclear and Chemical Sciences Division
Montana State University
Fort Lewis College
Forensic analysis of protein-containing samples. Bioinformatics of high-throughput proteomic and metabolomic datasets obtained from liquid chromatography-tandem mass spectrometry. High-resolution protein structure determination using solution NMR spectroscopy and elucidation of protein function through biochemical analysis.
Mason, K.E., T. Hamerly, A.M. Fischer and B. Bothner (2015). "Metabolomic comparison of post-anthesis barley flag leaves from near-isogenic germplasm differing in its senescence behavior."
Mason, K.E., J.K. Hilmer, W.S. Maaty, B.D. Reeves, P.A. Grieco, Bothner, B. Bothner and A.M. Fischer (2015). "Proteomic comparison of near-isogenic barley (Hordeum vulgare L.) germplasm differing in the allelic state of a major senescence QTL identifies numerous proteins involved in plant pathogen defense."
Mason, K. E., B. P. Tripet, D. Parrott, A. M. Fischer and V. Copie (2014). "1H, 13C, 15N backbone and side chain NMR resonance assignments for the N-terminal RNA recognition motif of the HvGR-RBP1 protein involved in the regulation of barley (Hordeum vulgare L.) senescence."
Tripet, B. P., K. E. Mason, B. J. Eilers, J. Burns, P. Powell, A. M. Fischer and V. Copie (2014). "Structural and biochemical analysis of the Hordeum vulgare L. HvGR-RBP1 protein, a glycine-rich RNA-binding protein involved in the regulation of barley plant development and stress response."