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Amanda Storm

Department of Biology
Assistant Professor

Office Phone: 828-227-3664
Office: Natural Science 130
Lab Website:

Postdoctoral Research and Teaching; James Madison University, Harrisonburg VA
Ph.D.; Miami University, Oxford OH
B.S.; Central State University, Wilberforce OH

Courses Taught
BIOL 240 Intro to Genetics
BIOL 493/593 Protein Systems and Bioinformatics
BIOL 480 Characterization of Bacterial Protein Structures

Research Description/Interests:
My primary research interest is in the diversity of function and regulation observed within enzyme families, primarily through use of a family of starch degradation enzymes, β-amylases, in the model plant Arabidopsis thaliana. Some research questions that stem from this interest include: (1) How are similar enzymes selectively regulated to restrict function to specific times and stress conditions; (2) How is degradation of starch in leaves altered throughout plant development to maximize growth and adapt to stress; (3) Are non-catalytic members within enzyme families serving regulatory roles?

I also have a collaborative project with the Center for Structural Genomics of Infectious Diseases (CSGID) that engages students in using bioinformatics tools to characterize crystal structures of proteins from pathogenic bacteria, pairing that information with in vitro activity assays to work towards publications about these new structures.

Undergraduate and graduate students in my lab will have projects related to these broad questions involving a variety of approaches, such as generation and characterization of transgenic and T-DNA knock-out plants, protein bioinformatics, enzyme kinetics, molecular cloning, protein over-expression and purification, and analysis of protein interactions and modifications.

Publications:   * indicates undergraduate author
Monroe, JD and Storm, AR. 2018. Review: The Arabidopsis β-amylase (BAM) gene family: Diversity of form and function. Plant Science 276: 163-170.

Monroe, JD; Pope, LE*; Breault, JS*; Berndsen, CE; and Storm, AR. 2018. Quaternary Structure, Salt Sensitivity, and Allosteric Regulation of β-AMYLASE2 From Arabidopsis thaliana. Front. Plant Sci. (9): 1176.

Storm, AR; Kohler, MR*; Berndsen, CE; Monroe, JD. 2018. Glutathionylation Inhibits the Catalytic Activity of Arabidopsis β-Amylase3 but Not That of Paralog β-Amylase1. Biochemistry 57 (5): 711-721.

Monroe, JD; Breault, JS*; Pope, LE*; Torres, CE*; Gebrejesust, TB*; Berndsen, CE; and Storm, AR. 2017. Arabidopsis b-Amylase2 is a K+-Requiring, Catalytic Tetramer with Sigmoidal Kinetics. Plant Physiology 175 (4): 1525-1535.

Monroe, JD; Storm, AR; Bradley, EM*; Lehman, MD*; Platt, SM*; Saunders, LK*; Schmitz, JM* and Torres, CE*. 2014. β-Amylase1 and β-Amylase3 Are Plastidic Starch Hydrolases in Arabidopsis That Seem to Be Adapted for Different Thermal, pH, and Stress Conditions. Plant Physiology 166: 1748-1763.


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