Matthew J. Whitley, PhD

Research Instructor

VA Medical Center University Drive C Building 6, Room 2A104
Pittsburgh, PA 15240
Phone: 412-360-6610

Education

B.S. (Chemistry, Biophysical Option), University of Arkansas, 2004
B.A. (German Language & Literature), University of Arkansas, 2004
Ph.D. (Biochemistry), University of North Carolina at Chapel Hill, 2010
Postdoctoral (Structural Biology), University of Pittsburgh, 2010-2015
 
Matthew J. Whitley, PhD

Labs

Dr. Whitley’s research is focused in the world of integrative structural biology/pharmacology.  He makes use of many tools in the field, chief among them X-ray crystallography, solution nuclear magnetic resonance spectroscopy, and small-angle X-ray scattering, to study proteins and protein complexes of biomedical relevance.  Currently, he is focused on understanding structure-function relationships in the pyruvate dehydrogenase multienzyme complex, a key metabolic complex that links glycolysis and the citric acid cycle.  The bacterial version of this complex is of interest as an antibiotic target, while malfunction of the human version has severe neurological consequences during development and after birth.  Other previous and ongoing work includes structural and biophysical characterization of mutants of gammaD-crystallin, which is associated with cataract formation in humans and many other species.

Journal Articles

Whitley MJ, Arjunan P, Nemeria NS, Korotchkina LG, Park YH, Patel MS, Jordan F and Furey W.  Pyruvate dehydrogenase complex deficiency is linked to regulatory loop disorder in the alphaV138M variant of human pyruvate dehydrogenase. J Biol Chem. 293: 13204-13213, 2018.
Boatz JC, Whitley MJ, Li M, Gronenborn AM and van der Wel PCA. Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH. Nat Commun. 8:15137, 2017.
Whitley MJ, Xi Z, Bartko JC, Jensen MR, Blackledge M and Gronenborn AM. A combined NMR and SAXS analysis of the partially folded cataract-associated V75D γD-Crystallin. Biophys J. 12:1135-114, 2017.
Xi Z, Whitley MJ and Gronenborn AM. Human βB2-Crystallin forms a face-en-face dimer in solution: An integrated NMR and SAXS study. Structure 25:496-505, 2017.
 
McDonald LR, Whitley MJ, Boyer JA and Lee AL. Colocalization of fast and slow timescale dynamics in the allosteric signaling protein CheY. J Mol Biol. 425:2372-2381, 2013.
Whitley MJ, Furey W, Kollipara S and Gronenborn AM. Burkholderia oklahomensis agglutinin is a canonical two-domain OAA-family lectin: structures, carbohydrate  binding and anti-HIV activity. FEBS J. 280:2056-2067, 2013.
Whitley MJ and Lee AL. Exploring the role of structure and dynamics in the function of chymotrypsin inhibitor 2. Proteins 79:916-924, 2011.
 
Whitley MJ and Lee AL. Frameworks for understanding long-range intra-protein communication. Curr Protein Pept Sci. 10:116-127, 2009.