Candice S. Klug, PhD

Candice S. Klug

Professor of Biophysics
Director of the National Biomedical EPR Center
Director of Biophysics Graduate Program

(414) 955-4015


  • Massachusetts Institute of Technology, BS, Chemistry (1994)
  • Medical College of Wisconsin, PhD, Biophysics (1999)
  • UCLA School of Medicine, Jules Stein Eye Institute, Postdoctoral Fellow in Ophthalmic Biophysical Chemistry (1999-2001)

Research Interests

My research interests currently center on protein structure and dynamics. I use the site-directed spin labeling (SDSL) EPR spectroscopy technique to study the functional dynamics of bacterial membrane and retinal proteins.

Lab Members


  • Site-Directed Spin Labeling of ArnT is a five-year, $1.1 million award from the National Institute of Allergy and Infectious Diseases to study the structure-function relationship of a previously uncharacterized bacterial membrane protein, ArnT, which is responsible for bacterial resistance to the antibiotic polymyxin.
  • Spin Labeling of MsbA is a four-year, $900,000 award from the National Institute of General Medical Sciences to study the functional dynamics of the bacterial ABC (ATP-binding-cassette) lipid transporter, MsbA, which transports lipids across the inner membrane of bacteria.

As part of these grants, the investigators will study the structure and functional dynamics of these two proteins as they bind their respective substrates. A more thorough understanding of the dynamics in the ArnT protein will help researchers develop strategies to overcome bacterial resistance to polymyxin and other antibiotics. A more thorough understanding of the dynamics in the MsbA protein will help researchers understand the molecular basis for multidrug resistance and diseases caused by malfunctioning proteins such as MsbA and will lead to novel therapeutic agents and gene therapies.

Open AllClose All
  Selected Publications
  • Rice, A.J., Alvarez, F.J.D, Schultz, K.M., KLUG, C.S., Davidson, A.L., Pinkett, H.W.  (2013) EPR Spectroscopy of MolB2C2-A Reveals Mechanism of Transport for a Bacterial Type II Molybdate Importer. J. Biol. Chem. 288, 21228-21235. **JBC Paper of the Week

  • Schultz, K.M., Feix, J.B., Klug, C.S.  (2013) Disruption of LptA oligomerization and affinity of the LptA-LptC interaction. Protein Sci. 22, 1639-1645.

  • Dellisanti, C.D., Ghosh, B., Hanson, S.M., Raspanti, J.M., Grant, V.A., Diarra, G.M., Schuh, A.M., Satyshur, K., Klug, C.S., Czajkowski, C. (2013) Site-directed spin labeling reveals pentameric ligand-gated ion channel gating motions. PLoS Biol. 11, e1001714.

  • Merten, J.A., Schultz, K.M., Klug, C.S.  (2012)  Concentration-dependent oligomerization and oligomeric arrangement of LptA.  Protein Sci. 21, 211-218.

  • Francis, D.J., Hubbell, W.L., Klug, C.S.   Probing Protein Secondary Structure using EPR:  Investigating a Dynamic Region of Visual Arrestin. Appl. Magn. Reson.  43, 405-419.

  • Schultz (Westfahl), K.W., Merten, J.A., KLUG, C.S.  (2011)Effects of the L511P and D512G mutations on the E. coli ABC transporter MsbA.  Biochemistry 50, 2594-2602

  • Schultz (Westfahl), K.W., Merten, J.A., KLUG, C.S.  (2011)  Characterization of the E506Q and H537A dysfunctional mutants in the ABC transporter MsbA.  Biochemistry 50: 3599-3608

  • Vishnivetskiy, S.A., Gimenez, L.E., Francis, D.J., Hanson, S.M., Hubbell, W.L., KLUG, C.S., Gurevich, V.V. (2011)  Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins. J. Biol. Chem. 286, 24288-24299.

  • Impellitteri NA, Merten JA, Bretscher LE, Klug CS. Identification of a functionally important loop in Salmonella typhimurium ArnT. Biochemistry 49:29-35 (2010).

  • Vishnivetskiy SA, Francis D, Van Eps N, Kim M, Hanson SM, KLUG CS, Hubbell WL, Gurevich VV. The role of arrestin alpha-helix I in receptor binding. J. Mol. Biol. 395:42-54 (2010).

  • Bretscher LE, Buchaklian AH, Klug CS. Spin-labeled lipid A. Anal. Biochem. 382:129-131 (2008).

  • Ferrante A, Anderson MW, Klug CS, Gorski J. HLA-DM mediates epitope selection by a "compare-exchange" mechanism when a potential peptide pool is available. PLoS ONE 3:e3277 (2008).

  • Hanson SM, Dawson ES, Francis DJ, Van Eps N, Klug CS, Hubbell WL, Meiler J, Gurevich VV. A model for the solution structure of the rod arrestin tetramer. Structure 16:924-934 (2008).

  • Klug CS, Feix JB. Methods and applications of site-directed spin labeling EPR spectroscopy. Methods Cell Biol. 84:617-658 (2008).

  • Orelle C, Ayvaz T, Everly RM, Klug CS, Davidson AL. Both maltose-binding protein and ATP are required for nucleotide-binding domain closure in the intact maltose ABC transporter. Proc. Natl. Acad. Sci. USA 105:12837-12842 (2008).

  • Westfahl KM, Merten JA, Buchaklian AB, Klug CS. Functionally important ATP binding and hydrolysis sites in E. coli MsbA. Biochemistry 47:13878-13886 (2009).

Medical College of Wisconsin
8701 Watertown Plank Road
Milwaukee, WI 53226
(414) 955-8296
Directions & Maps
© 2016

Page Updated 01/22/2016