Pam Twigg



Dr. Pam Twigg

Lecturer, Chemistry


My research focus is on the structural and biophysical characterization of proteins, using methods such as x-ray crystallography, NMR spectroscopy, circular dichroism, calorimetry, and fluorescence spectroscopy. In particular, I am interested in the protein-protein interactions and function of proteins related to the pathology of Huntington's Disease, a genetic movement disorder.

I’ve been a Research Assistant Professor at the University of Alabama in Huntsville since 2004.

Curriculum Vitae


  • Ph.D., Molecular Biophysics, Florida State University, 2001
  • M.S., Biomedical Engineering, University of Alabama at Birmingham, 1986
  • B.S., Chemical Engineering, Auburn University, 1982

Classes Taught


  • Helms, K. M., Wilson, R. C., Ogungbe, I. V., Setzer, W. N., and Twigg, P. D. 2011. "Vitexin Inhibits Polyubiquitin Synthesis by the Ubiquitin-conjugating Enzyme E2-25K." Natural Product Communications, 6(10), 1411-1416.
  • Wilson, R. C., Edmondson, S. P., Flatt, J. W., Helms, K., and Twigg, P. D. 2011. “The E2-25K Ubiquitin-associated (UBA) Domain Aids in Polyubiquitin Chain Synthesis and Linkage Specificity.” Biochem. Biophys. Res. Com., 405(4), 662-666.
  • Twigg, P. D., Lamb, N. E., DuBreuil, R. M., and Zahorchak, R. 2011. “APPLE for the Teacher: Scientists in the Classroom. From Grass Roots to Productive Orchard.” The American Biology Teacher, 73(8), 444-448.
  • Wilson, R. C., Hughes, R. C., Flatt, J. W., Meehan, E. J., Ng, J. D., and Twigg, P. D. 2009. “The crystal structure of full-length ubiquitin-conjugating enzyme E2-25K (huntingtin-interacting protein 2).” Acta Cryst., F65, 440-444.
  • Wilson, R. C., Hughes, R. C., Curto, E. V., Ng, J. D., and Twigg, P. D. 2007. “Backbone 1H, 15N, and 13C Resonance Assignments and Secondary Structure of a Novel Protein OGL-20Pt-358 from HyperthermophileThermococcus thioreducens sp. Nov.” Molecules and Cells, 24(3), 437-440.
  • Twigg, P. D., G. Parthasarathy, L. Guerrero, T. M. Logan, and D. L. D. Caspar. 2001. “Disordered to Ordered Folding in the Regulation of Diphtheria Toxin Repressor Activity.” Proc. Natl. Acad. Sci. USA, 98, 11259-64.
  • Wang, G., G. P. Wylie, P. D. Twigg, D. L. D. Caspar, J. R. Murphy, and T. M. Logan. 1999. “Solution Structure and Peptide Binding Studies of the C-Terminal SH3-Like Domain of the Diphtheria Toxin Repressor Protein.” Proc. Natl. Acad. Sci. USA, 96, 6119-6124.
  • Twigg, P. D., G. P. Wylie, G. Wang, D. L. D. Caspar, J. R. Murphy, and T. M. Logan. 1999. “Expression and Assignment of the 1H, 15N, and 13C Resonances of the C-terminal Domain of the Diphtheria Toxin Repressor.” J. Biomolecular NMR, 13(2), 197-198.
  • Wardell, M. R., Skinner, R., Carter, D. C., Twigg, P. D., & Abrahams, J.-P. 1997. “Improved diffraction of antithrombin crystals grown in microgravity.” Acta Cryst.D, 53, 622-625.
  • Ho, J.X., E.W. Holowachuk, E.J. Norton, P.D. Twigg, and D.C. Carter. 1993. “X-ray and Primary Structure of Horse Serum Albumin (Equus caballus) at 0.27-nm Resolution.” Eur. J. Biochem., 215, 205-212.
  • Carter, D.C., He, X.-M., Munson, S.H., Twigg, P.D., Gernert, K.M., Broom, M.B., and Miller, T.Y. 1989. “Three-Dimensional Structure of Human Serum Albumin.” Science, 244, 1195-1198.