Jack J. Skalicky, PhD

Research Interests

  • Nuclear Magnetic Resonance
  • Nuclear Magnetic Resonance, Biomolecular


  • English

Academic Information

  • Departments: Biochemistry - Research Associate Professor

Academic Office Information

  • 801-585-7363
  • Emma Eccles Jones Research Building
    15 North Medical Drive East, Room: 3730
    Salt Lake City, UT 84112

Academic Bio

Jack Skalicky, PhD, is a research professor in the Department of Biochemistry at the University of Utah. He is the director of the Health Sciences Nuclear Magnetic Resonance (NMR) core and an investigator at the Huntsman Cancer Institute.

Dr. Skalicky is a nuclear magnetic resonance expert, and he has an independent research program that focuses on the structure-dynamics-function relationship of a model enzyme system. He also uses NMR in structural biology and has made significant contribution to our current understanding of how Microtubule Interacting and Trafficking (MIT)-containing proteins and ESCRT-III proteins bind one another, interactions that are important in HIV-1 budding, cytokinesis, and multivescicular body formation. As NMR core director, Skalicky supports the work of cancer center colleagues.

Jack Skalicky received his BS from the University of Wisconsin - River Falls and a PhD from the University of Colorado - Boulder. He completed postdoctoral fellowships at the University of British Columbia and University at Buffalo - SUNY, and he led the solution NMR program at the National High Magnetic Field Laboratory in Tallahassee, FL.

Education History

Type School Degree
Postdoctoral Fellowship The State University at Buffalo
Biomolecular NMR
Postdoctoral Fellow
Postdoctoral Fellowship University of British Columbia
Biomolecular NMR
Postdoctoral Fellow
Doctoral Training University of Colorado
Graduate Training University of Northern Colorado
Undergraduate University of Wisconsin
Biology and Chemistry

Global Impact

Education History

Type School Degree Country
Postdoctoral Fellowship University of British Columbia
Biomolecular NMR
Postdoctoral Fellow Canada

Selected Publications

Journal Article

  1. Green BR, Gajewiak J, Chhabra S, Skalicky JJ, Zhang MM, Rivier JE, Bulaj G, Olivera BM, Yoshikami D, Norton RS (2016). Structural Basis for the Inhibition of Voltage-gated Sodium Channels by Conotoxin muO section sign-GVIIJ. J Biol Chem, 291(13), 7205-20.
  2. Chapman BK, Davulcu O, Skalicky JJ, Bruschweiler RP, Chapman MS (2015). Parsimony in Protein Conformational Change. Structure, 23(7), 1190-8.
  3. Caballe A, Wenzel DM, Agromayor M, Alam SL, Skalicky JJ, Kloc M, Carlton JG, Labrador L, Sundquist WI, Martin-Serrano J (2015). ULK3 regulates cytokinetic abscission by phosphorylating ESCRT-III proteins. eLife, 4, e06547.
  4. Davulcu O, Niu X, Bruschweiler-Li L, Bruschweiler R, Skalicky JJ, Chapman MS (2014). Backbone resonance assignments of the 42 kDa enzyme arginine kinase in the transition state analogue form. Biomolecular N M R Assignments, 8(2), 335-8.
  5. Skalicky JJ, Arii J, Wenzel DM, Stubblefield WM, Katsuyama A, Uter NT, Bajorek M, Myszka DG, Sundquist WI (2012). Interactions of the human LIP5 regulatory protein with endosomal sorting complexes required for transport. J Biol Chem, 287(52), 43910-26.
  6. Wei X, Henriksen NM, Skalicky JJ, Harper MK, Cheatham TE 3rd, Ireland CM, Van Wagoner RM (2011). Araiosamines A-D: tris-bromoindole cyclic guanidine alkaloids from the marine sponge Clathria (Thalysias) araiosa. J Org Chem, 76(14), 5515-23.
  7. Davulcu O, Skalicky JJ, Chapman MS (2011). Rate-limiting domain and loop motions in arginine kinase. Biochemistry, 50(19), 4011-8.
  8. Niu X, Bruschweiler-Li L, Davulcu O, Skalicky JJ, Bruschweiler R, Chapman MS (2011). Arginine kinase: joint crystallographic and NMR RDC analyses link substrate-associated motions to intrinsic flexibility. J Mol Biol, 405(2), 479-96.
  9. Nguyen TK, Tran VM, Victor XV, Skalicky JJ, Kuberan B (2010). Characterization of uniformly and atom-specifically (13)C-labeled heparin and heparan sulfate polysaccharide precursors using (13)C NMR spectroscopy and ESI mass spectrometry. Carbohydr Res, 345(15), 2228-32.
  10. Paulsen RB, Seth PP, Swayze EE, Griffey RH, Skalicky JJ, Cheatham TE 3rd, Davis DR (2010). Inhibitor-induced structural change in the HCV IRES domain IIa RNA. Proc Natl Acad Sci U S A, 107(16), 7263-8.
  11. Gowd KH, Yarotskyy V, Elmslie KS, Skalicky JJ, Olivera BM, Bulaj G (2010). Site-specific effects of diselenide bridges on the oxidative folding of a cystine knot peptide, omega-selenoconotoxin GVIA. Biochemistry, 49(12), 2741-52.