Faculty & Research // Department of Chemistry and Biochemistry // University of Notre Dame

Biography

B.S. Cornell University, A&EP

Ph.D. Univ of Michigan, Biophysics

Postdoctoral Fellow: ETH-Zuerich Physical Chemistry

Senior Staff Investigator: Vertex Pharmaceuticals, Inc. (1994-2003) Cambridge MA, Structural Biology

Asst Prof. Univ of Notre Dame 2003- present

Research Interests

Biophysics, NMR Spectroscopy, Protein and Ligand Dynamics

The Peng Lab works at the interface of the physical and biological sciences to illuminate the role of protein and ligand conformational dynamics in biomolecular recognition and molecular evolution.

Our main experimental tool is multi-dimensional NMR. We focus on both methods development, and applications to several proteins of therapeutic interest. A long term goal is to develop a more fundamental understanding of signal transduction that includes structural ensembles and dynamics. This has relevance for understanding the evolution of protein-protein interaction networks as well as drug design. We complement our NMR studies with molecular dynamics calculations, protein biochemistry, and collaborations with groups focused on theory and medicinal chemistry.

Recent Papers

Peng JW, Wilson BD, Namanja AT (2009). Mapping the dynamics of ligand reorganization via 13CH3 and 13CH2 relaxation dispersion at natural abundance. J Biolmol NMR 45(1-2):171-83. Link

Pasat G, Zintsmaster JS, Peng JW (2008). Direct 13C-detection for carbonyl relaxation studies of protein dynamics. J. Magn. Reson. 193(2):226-32. Link

Zintsmaster JS, Wilson BD, Peng JW (2008). Dynamics of ligand binding from 13C NMR relaxation dispersion at natural abundance. J. Am. Chem. Soc. 130(43): 14060-1. Epub 2008 Oct 4. Link

Namanja AT, Peng T, Zintsmaster JS, Elson AC, Shakour MG, Peng JW (2007). Substrate recognition reduces side-chain flexibility for conserved hydrophobic residues in human Pin1. Structure 15(3): 313-27. Link

Peng T., Zintsmaster JS, Namanja AT, Peng JW (2007). Sequence-specific dynamics modulate recognition specificity in WW domains. Nat Struct Mol Biol Apr; 14(4):325-31. Epub 2007 Mar 4 Link

Peng, JW (2003). New probes of ligand flexibility in drug design: Transferred cross-correlated ¹³C CSA-dipolar relaxation at natural abundance. J. Am. Chem. Soc. 125: 11116-11130. Link