The Frederick lab is interested in determining how cellular environments affect protein structures with a particular interest in proteins that are metastable or instrinsically disordered, such as those involved neurodegenerative diseases.

Kendra received her B.S. with Honors from the University of Michigan in Biochemistry and French Language and Literature.  Working with David Ballou and Bruce Palfey, she determined the kinetics of the chemical and conformational transitions that control the reductive half-reaction of the flavoprotein p-hydroxybenzoate hydroxylase using transient state kinetics and kinetic isotope effects.  She then earned a Diplôme d’études Approfondis (M.S.) from the Université de Paris XI in protein structure, function and engineering.  She used suicide inhibitors to investigate the mechanism of flavin reduction in hydroxyacid oxidases with Florence Lederer at the Centre National de la Recherche Scientifique (CNRS) in Gif-sur-Yvette.

Kendra did her Ph.D. with A. Joshua Wand in the department of Biochemistry and Molecular Biophysics at the University of Pennsylvania.  She investigated the contribution that changes in protein entropy make to the overall energetics of ligand binding using solution state NMR relaxation techniques.  Most significantly, her work established that the changes in dynamic disorder of the protein side chains were the energetic driver of the entropy term of ligand binding.

Kendra was a post-doctoral fellow with Susan Lindquist at the Whitehead Institute.  Working in close collaboration with Robert Griffin’s group in MIT Chemistry and the Francis Bitter Magnet Labs, she developed technology to obtain atomic structural level information about proteins in their native contexts and is applying it to protein folding events, such as those involved in macromolecular protein assemblies that drive neurodegenerative disease.  This work was supported by a NRSA from the NIH as well as an HHMI fellowship from the Life Science Research Foundation.

Since joining the faculty of UT Southwestern in 2015, Dr. Frederick has been implementing an integrated structural biology approch encompassing NMR spectroscopy, protein chemistry and yeast genetics to determine the structures, dynamics and energergetics of protein folding in complex physiological environments such as those involved in the initiation and progression of human disease.


University of Michigan (2000), Biochemistry
Graduate School
University of Paris - France (2001), Engineering
Graduate School
University of Pennsylvania (2006), Biochemistry

Research Interest

  • Neurodegenerative diseases
  • Protein folding and structure in cellular environments
  • Sensitivity-enhanced solid-state NMR


Featured Publications LegendFeatured Publications

Characterization of the fast dynamics of protein amino acid side chains using NMR relaxation in solution.
Igumenova TI, Frederick KK, Wand AJ Chem. Rev. 2006 May 106 5 1672-99
Arylamide derivatives as peptidomimetic inhibitors of calmodulin.
Yin H, Frederick KK, Liu D, Wand AJ, Degrado WF Org. Lett. 2006 Jan 8 2 223-5
Kinetics of proton-linked flavin conformational changes in p-hydroxybenzoate hydroxylase.
Frederick KK, Palfey BA Biochemistry 2005 Oct 44 40 13304-14
Changes in calmodulin main-chain dynamics upon ligand binding revealed by cross-correlated NMR relaxation measurements.
Wang T, Frederick KK, Igumenova TI, Wand AJ, Zuiderweg ER J. Am. Chem. Soc. 2005 Jan 127 3 828-9
Control of adenosylmethionine-dependent radical generation in biotin synthase: a kinetic and thermodynamic analysis of substrate binding to active and inactive forms of BioB.
Ugulava NB, Frederick KK, Jarrett JT Biochemistry 2003 Mar 42 9 2708-19
Role of protein flexibility in the catalytic cycle of p-hydroxybenzoate hydroxylase elucidated by the Pro293Ser mutant.
Palfey BA, Basu R, Frederick KK, Entsch B, Ballou DP Biochemistry 2002 Jul 41 26 8438-46
Protein dynamics control proton transfers to the substrate on the His72Asn mutant of p-hydroxybenzoate hydroxylase.
Frederick KK, Ballou DP, Palfey BA Biochemistry 2001 Apr 40 13 3891-9

Honors & Awards

  • NSF CAREER award
  • Searle Scholar
  • HHMI Fellow of the Life Science Research Foundation
  • NIH NRSA (F32)
  • Winegrad Award for Outstanding Dissertation
  • Sokol Chemistry Scholarship