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

Univ of Notre Dame 2003-

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 bio-molecular dynamics in molecular recognition and evolution.

Our main experimental tool is multi-dimensional NMR. We focus on both methods development, and applications to several proteins of therapeutic interest. Our long term interests include: (i) getting a fundamental understanding of signal transduction and protein evolution that includes conformational ensembles and dynamics. This has relevance for understanding protein-protein interaction networks and drug resistance; (ii) new methods for including flexibility information in iterative drug design. We complement our NMR studies with molecular dynamics calculations, protein biochemistry, and collaborations with groups focused on medicinal chemistry.

Recent Papers

Namanja AT, Wang XJ, Xu B, Mercedes-Camacho AY, Wilson KA, Etzkorn FE, and Peng JW (July 11, 2011). Stereo-specific gating of functional motions in Pin1. Proc Natl Acad Sci USA Early Edition: doi:10.1073/pnas.1019382108

Morcos F, Chatterjee S, McClendon CL, Brenner PR, Lopez-Rendon R, Zintsmaster J, Ercsey-Ravasz M, Sweet CR, Jacobson MP, *Peng JW, *Izaguirre JA (2010). Modeling conformational ensembles of slow functional motions in Pin1-WW. PLoS Comput Biol 2010 Dec 2;6(12) e1001015

Link

Namanja AT, Wang XJ, Xu B, Mercedes-Camacho AY, Wilson BD, Wilson KA, Etzkorn FA, Peng JW (2010). Toward flexibility-activity relationships by NMR spectroscopy: Dynamics of Pin1 ligands. Epub 2010 April 1

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