Candice S. Klug, PhD

Professor; Director, National Biomedical EPR Center; Program Director, Biophysics Graduate Program

Locations

Biophysics
MFRC 2026

Contact Information

Education

Postdoctoral Fellow in Ophthalmic Biophysical Chemistry, UCLA School of Medicine, Jules Stein Eye Institute, Los Angeles, CA, 1999-2001
PhD, Biophysics, Medical College of Wisconsin, Milwaukee, WI, 1999
BS, Chemistry, Massachusetts Institute of Technology, Cambridge, MA, 1994

Biography

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

                
                    Methodologies and Techniques
                

                    Adenosine Triphosphatases
Amino Acid Motifs
ArnT
Arrestin
Arrestins
ATP-Binding Cassette Transporters
Bacterial Proteins
electron paramagnetic resonance spectroscopy
Electron Spin Resonance Spectroscopy
Escherichia coli Proteins
Lipid A
Lipopolysaccharides

            

                
                    Leadership Positions
                

                    Associate Director, National Biomedical EPR Center, 2014-2016
Chair, Graduate School Curriculum and Programs Committee, 2010-2013
Chair, Women in Science Advisory Committee, 2011 - 2016
Chair, Women's Faculty Council, 2006-2007
Director, National Biomedical EPR Center, 2016 - present
President, MCW Faculty Council, 2016-2017
Program Director, Biophysics Graduate Program, 2013 - present
Training Program Director, National Biomedical EPR Center, 2003-present 

            

                
                    MCW Program / Core Facilities
                

                    Biophysics Graduate Program
Interdisciplinary Program in the Biomedical Sciences
National Biomedical EPR Center

            

Research Interests

LptA-Mediated Transport of LPS is an R01 award from the National Institute of General Medical Sciences to study how LptA transports LPS. Genetic screenings, laser light scattering analyses, EPR spectroscopy studies, and isothermal titration calorimetry measurements are used to provide detailed insights into the mechanisms of LPS transport across the periplasm of Gram-negative bacteria.

National Biomedical EPR Center is a P41 award from the National Institute of Biomedical Imaging and Bioengineering. The mission of the EPR Center is to serve the community of EPR spectroscopists by development of advanced EPR instrumentation and new EPR methodology.

Disruption of the E. coli LptC dimerization interface and characterization of lipopolysaccharide and LptA binding to monomeric LptC.

(Schultz KM, Fischer MA, Noey EL, Klug CS.) Protein Sci. 2018 08;27(8):1407-1417.
Characterization of and lipopolysaccharide binding to the E. coli LptC protein dimer.

(Schultz KM, Klug CS.) Protein Sci. 2018 02;27(2):381-389.
High-pressure EPR spectroscopy studies of the lipopolysaccharide transport proteins LptA and LptC.

(Schultz KM, Klug CS.) Appl Magn Reson. 2017 Dec;48(11-12):1341-1353.
Structural basis of arrestin-3 activation and signaling.

(Chen Q, Perry NA, Vishnivetskiy SA, Berndt S, Gilbert NC, Zhuo Y, Singh PK, Tholen J, Ohi MD, Gurevich EV, Brautigam CA, Klug CS, Gurevich VV, Iverson TM.) Nat Commun. 2017 11 10;8(1):1427.
Lipopolysaccharide binding to the periplasmic protein LptA.

(Schultz KM, Lundquist TJ, Klug CS.) Protein Sci. 2017 Aug;26(8):1517-1523.
Directed evolution provides insight into conformational substrate sampling by SrtA.

(Suliman M, Santosh V, Seegar TCM, Dalton AC, Schultz KM, Klug CS, Barton WA.) PLoS One. 2017;12(8):e0184271.
Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation.

(Petrou VI, Herrera CM, Schultz KM, Clarke OB, Vendome J, Tomasek D, Banerjee S, Rajashankar KR, Belcher Dufrisne M, Kloss B, Kloppmann E, Rost B, Klug CS, Trent MS, Shapiro L, Mancia F.) Science. 2016 Feb 05;351(6273):608-12.
Full engagement of liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporter.

(Alvarez FJ, Orelle C, Huang Y, Bajaj R, Everly RM, Klug CS, Davidson AL.) Mol Microbiol. 2015 Dec;98(5):878-94.
Identification of receptor binding-induced conformational changes in non-visual arrestins.

(Zhuo Y, Vishnivetskiy SA, Zhan X, Gurevich VV, Klug CS.) J Biol Chem. 2014 Jul 25;289(30):20991-1002.
Active conformations of arrestins: Expected and unexpected changes

(Bandyopadhyay A, Zhuo Y, Hubbell WL, Klug CS, Gurevich VV, Ernst OP.) The Structural Basis of Arrestin Functions. 24 May 2017:159-173.
GPCR footprint on arrestins and manipulation of receptor specificity

(Vishnivetskiy SA, Hubbell WL, Klug CS, Gurevich VV.) The Structural Basis of Arrestin Functions. 24 May 2017:133-140.
Overview of arrestin mediated signaling with receptors and non-receptor binding partners

(Zhuo Y, Klug CS.) The Structural Basis of Arrestin Functions. 24 May 2017:19-29.

Candice S. Klug, PhD