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

Orientation of aromatic residues in amyloid cores: structural insights into prion fiber diversity.
Reymer A, Frederick KK, Rocha S, Beke-Somfai T, Kitts CC, Lindquist S, Nordén B Proc. Natl. Acad. Sci. U.S.A. 2014 Dec 111 48 17158-63
The role of conformational entropy in molecular recognition by calmodulin.
Marlow MS, Dogan J, Frederick KK, Valentine KG, Wand AJ Nat. Chem. Biol. 2010 May 6 5 352-8
Re-evaluation of the model-free analysis of fast internal motion in proteins using NMR relaxation.
Frederick KK, Sharp KA, Warischalk N, Wand AJ J Phys Chem B 2008 Sep 112 38 12095-103
Characterization of the backbone and side chain dynamics of the CaM-CaMKIp complex reveals microscopic contributions to protein conformational entropy.
Frederick KK, Kranz JK, Wand AJ Biochemistry 2006 Aug 45 32 9841-8
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