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Edwin Li, Ph.D.

Assistant Professor
Office: Science Center 125
Research Lab: Science Center 109
Phone: 610-660-1888
Fax: 610-660-1832


  • B.A.  in Chemical Engineering (1994), Rutgers University, NJ
  • M.S. in Chemical Engineering (1997), University of Rhode Island, RI
  • Ph.D. in Chemical Engineering (2001), University of Rhode Island, RI

Professional Experience

Post-Doctoral Research Fellow (2002-2005), Johns Hopkins University, Baltimore, MD

Assistant Research Scientist (2006-2009), Johns Hopkins University, Baltimore, MD

Visiting Research Fellow (2009-2010), Technical University of Munich, Germany

Assistant Professor (2010-present), Department of Biology, Saint Joseph‘s University, Philadelphia, PA

Courses Taught

  • Cells
  • Cellular and Molecular Biophysics  


Assembly of the m2 tetramer is strongly modulated by lipid chain length. Schick S, Chen L, Li E, Lin J, Koeper I, Hristova K. Biophys J 2010, 99(6):1810-7

Receptor tyrosine kinase transmembrane domains: Function, dimer structure and dimerization energetics. Li E, Hristova, K. Cell Adh Migr 2010, 4(2):24954

Increased expression of the integral membrane protein ErbB2 in Chinese hamster ovary cells expressing the anti-apoptotic gene Bcl-xl.  O'Connor S, Li E, He L, Placone J, Baycin D, Betenbaugh MJ, Hristova K. Protein Expr Purif 2009, 67(1):41-7

Utility of surface-supported bilayers in studies of transmembrane helix dimerization. Li E, Merzlyakov M, Lin J, Searson P, Hristova K.  J Struct Biol 2008, 168(1):53-60

Quantitative measurements of protein interactions in a crowded cellular environment. Li E, Placone J, Merzlyakov M, Hristova K.  Anal Chem 2008, 80(15):5976-85

Spectral Forster resonance energy transfer detection of protein interactions in surface-supported bilayers. Merzlyakov M, Li E, Casas R, Hristova K. Langmuir 2006, (16):6986-92

Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies. Li E, Hristova K.  Biochemistry, 2006, 45(20):6241-51

FGFR3 dimer stabilization due to a single amino acid pathogenic mutation. Li E, You M, Hristova K.  J Mol Biol 2006, 356(3):600-12

Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Forster resonance energy transfer suggest weak interaction between fibroblast growth factor receptor 3 (FGFR3) transmembrane domains in the absence of extracellular domains and ligands. Li E, You M, Hristova K.  Biochemistry 2005, 44(1):352-60

Imaging Forster resonance energy transfer measurement of transmembrane helix interactions in lipid bilayers on a solid support. Li E, Hristova K.  Langmuir 2004, 20:9053-9060