Adrienne Loh profile photo

Adrienne Loh

Specialty area(s)

Interim Associate Dean, School of Education, Aug. 2017-present                                                                                                     

Chair: Department of Educational Studies, Sept. 2014-present

Professor, Chemistry & Biochemistry: Physical & Biophysical Chemistry, NMR Spectroscopy, Peptide & Protein Structure

Brief biography

I grew up just outside of Boston, MA. After attending McGill University (B.Sc. - Chemistry & Mathematics; Montreal, CA) and Cornell University (M.S. and Ph.D. Biophysical Chemistry; Ithaca, NY), I worked for one year as an Adjunct Professor of Chemistry at St. Bonaventure University (Olean, NY). I joined the Chemistry department at UW-L in 1997, earning tenure in 2002, and promotion to Full Professor in 2010. In Fall 2014 I was appointed Interim Chair of the Educational Studies Department, and was elected to a three year term in 2016 (2016-2019). In Fall 2017 I began my appointment as Interim Associate Dean of the School of Education, Professional and Continuing Education.  I continue to serve as Educational Studies Chair, and hold my position as Professor in Chemistry & Biochemistry in my work with several research students in my lab.

My research program involves undergraduate students in investigations of the structures of peptides and proteins, and the interactions of model antibiotic peptides with lipid environments. I also have collaborations with research groups at Cornell University (R.Oswald, Dept. Molecular Medicine) and Universite Pierre et Marie Curie in Paris (O. Lequin, Laboratoire des Biomolecules).  When I'm not in La Crosse, I am likely by the ocean, in France, or both.


B.Sc. Chemistry & Mathematics - McGill University (Montreal, CA) 1989
M.S. Biophysical Chemistry - Cornell University (Ithaca, NY) 1991
Ph.D. Biophysical Chemistry - Cornell University (Ithaca, NY) 1995

Teaching history

CHM 103 (General Chemistry I) - lecture & lab
CHM 104 (General Chemistry II) - lecture & lab
CHM 309 (Physical Chemistry I)
CHM 310 (Physical Chemistry II)
CHM 313 (Physical Chemistry Laboratory)
CHM 407 (Biophysical Chemistry)

Professional history

Université Pierre et Marie Curie, Paris, France:  
Visiting Researcher, Laboratoire des BioMolécules: July – Dec., 2013 (Sabbatical); June – July: 2014, 2015, 2016

Cornell University, Ithaca, NY
Visiting Associate Professor, Dept. Molecular Medicine:  May – Aug., 2000-2005 & 2008

St. Bonaventure University, Olean, NY
Adjunct Faculty, Dept. Chemistry: Aug. 1995-May 1996                                                                                                                                      

Research and publishing

Infectious diseases are the second leading cause of death worldwide and the third leading cause of death in economically advantaged countries. There is increasing evidence of persistent infections caused by microorganisms that are resistant to existing antibiotics, resulting in a serious threat to public health worldwide. Peptide antibiotics offer one promising solution because they act by perturbing cell membranes rather than acting on a specific protein target, making resistance more difficult to develop. Existing designed and natural peptide antibiotics tend to be helical in shape, and have both polar (hydrophiphilic) and non-polar (hydrophobic) regions.In my research program, we are trying to understand how to design peptide antibiotics with predictable structures, and to relate their structures to their lipid binding and cell-killing effectiveness. In particular, we are examining the roles of steric hindrance (“size”, “bulkiness”) and placement of charges (positive and/or negative) on helical structure.

Students in my group use a variety of methods to study these model peptide antibiotics. Some students use NMR spectroscopy to investigate the hydrogen-bonding networks by measuring H/D exchange kinetics or changes in amide proton chemical shift. Some students use NMR data to calculate the 3-dimensional structures of the peptides. Others use circular dichroism (CD) spectrscopy to monitor global structure or ITC (isothermal titration calorimetry) to measuring the thermodynamics of peptide-lipid binding. Soon to come are measurements of antimicrobial acitivity and cytotoxicity.

I am also interested in protein dynamics and the role that protein motions and conformation play in signal transduction. To this end, I have been working with R. Oswald at Cornell University, using NMR spectroscopy and isothermal titration calorimetry to study rote in-ligand binding interactions.

Selected Publications:

Martinez, M., Ahmed, A. H., Loh, A. P. Loh, and Oswald, R. E., (2014) Thermodynamics and Mechanism of the Interaction of Willardiine Partial Agonists with a Glutamate Receptor: Implications for Drug Development, Biochemistry, 53 (23), pp 3790–3795.

Ahmed, A. H., Thompson, M. D., Fenwick, M. E., Romero, B., Loh, A. P., Jane, D. E., Sondermann, H., Oswald, R. E. (2009). Mechanisms of Antagonism of the GluR2 AMPA Receptor: Structure and Dynamics of the Complex of Two Willardiine Antagonists with the Glutamate Binding Domain. Biochemistry, 48(18), 3894-3903.

Ahmed, A. H., Loh, A. P., Jane, D. E., Oswald, R. E. (2007). Dynamics of the S1S2 Glutamate Binding Domain of GluR2 Measured using 19F NMR Spectroscopy. J. Biol. Chem./ASBMB, 282(17), 12773-12784.

Oswald, R. E., Ahmed, A., Fenwick, M. K., Loh, A. P. (2007). Structure of Glutamate Receptors. in Current Drug Targets Current Drug Targets, 8, 573-582.

Adams, P. D., Loh, A. P., Oswald, R. E. (2004). Backbone Dynamics of an Ocogenic Mutant of Cdc42Hs shows Increased Flexibility at the Nucleotide Binding Site. Biochemistry, 43, 9968-9977.

Loh, A. P., Pawley, N., Nicholson, L. K., Oswald, R. E. (2001). An Increase in Sidechain Entropy Facilitates Effector Binding: NMR Characterization of the Methyl Group Dynamics in Cdc42Hs. Biochemistry/ACS, 40, 4590-4600.

Loh, A. P., Guo, W., Nicholson, L. K., Oswald, R. E. (1999). Backbone Dynamics of Inactive, Active, and Effector-Bound Cdc42Hs from Measurements of 15N Relaxation Parameters at Multiple Field Strengths. Biochemistry/ACS, 38, 12547-12557.