Kendra Frederick | Principle Investigator

kendra.frederick at

Kendra’s Curriculum Vitae

The Frederick lab is interested in determining how cellular environments affect protein structures with a particular interest in proteins that are metastable or intrinsically 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 moved to the University of Pennsylvania for her Ph.D. where she investigated the contribution that changes in protein entropy make to the overall energetics of ligand binding using solution state NMR relaxation techniques in the laboratory of A. Joshua Wand in the department of Biochemistry and Molecular Biophysics.   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.  Her thesis was recognized with the Winegrad Award for Outstanding Dissertation.

Kendra pursued postdoctoral training at the Whitehead Institute with Susan Lindquist.  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.

In 2015, Dr. Frederick established her independent group at UT Southwestern, where she is 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.  Dr. Frederick has received a number of distinctions including being named a Searle Scholar, a CPRIT Scholar and the Lupe Murchison Foundation Scholar in Medical Research.