S. WALTER ENGLANDER, Ph.D.

Jacob Gershon-Cohen Professor of Medical Science
Professor of Biochemistry and Biophysics
Member, National Academy of Sciences
Member, American Academy of Arts & Sciences
Fellow of The Biophysical Society
Fellow of American Association for the Advancement of Science

Location: 1005-09 Stellar-Chance Building
Tel: (215) 898-8042
Fax: (215) 898-2415
Email: engl@mail.med.upenn.edu

Ph.D. University of Pittsburgh (1958)

Englander Lab

DESCRIPTION OF RESEARCH INTERESTS:

Dr. Englander's laboratory is interested in biophysical studies of protein structure, function, folding, misfolding, and amyloid. Methods in use include the range of protein biophysical techniques including 2D NMR, chemical and spectroscopic approaches, analytical ultracentrifugation, electron microscopy, mass spectrometry, mutational analysis.

This laboratory has led in the development and use of hydrogen exchange (HX) approaches in protein and nucleic acid studies. HX measurements provide many dozens of probe points that are sensitive to structure, structure change, internal dynamics, energy, and functional interactions at identifiable positions throughout all macromolecules. The lab has developed and is using special hydrogen exchange methods that can measure the specific parts of any protein involved in any function, the protein folding process as it occurs on a sub-second time scale, the energetic stability of individual interactions, structure change, structure and dynamics in insoluble amyloids, etc.

RECENT REPRESENTATIVE PUBLICATIONS:

  1. Krishna, M.M.G., S.W. Englander (2007) A unified mechanism for protein folding: Predetermined pathways and optional errors. Protein Sci. 16:449-464. pdf file
  2. Krishna, M. M. G., Maity, H., Rumbley, & Englander, S. W. (2007) Branching in the sequential folding pathway of cytochrome c. Protein Sci. 16:1-11. pdf file
  3. Englander, S.W. (2006) Hydrogen exchange and mass spectrometry: a historical perspective. J. Amer. Soc. Mass Spec 17:1481-1489. pdf file
  4. Krishna, M.M.G., H. Maity, J.N. Rumbley, Y. Lin, and S.W. Englander (2006). Order of steps in the cytochrome c folding pathway: Evidence for a sequential stabilization mechanism. J. Mol. Biol. 359:1410-1419. pdf file
  5. Maity, H., J.N. Rumbley, S.W. Englander (2006) Functional role of a protein foldon: An W-loop foldon controls the alkaline transition in cytochrome c. Proteins 63:349-355. pdf file
  6. Del Mar, C., E.A. Greenbaum, L. Mayne, S.W.Englander, and V.L. Woods, Jr. (2005) Structure and properties of α-synuclein and other amyloids determined at the amino acid level. Proceedings of the National Academy of Sciences 102:15477-15482. pdf file
  7. Greenbaum, E.A., C.L. Graves, A.J. Mishizen-Eberz, M.A. Lupoli, D.R. Lynch, S.W. Englander, P.H. Axelsen, and B.I. Giasson (2005) The E46K mutation in α-synuclein increases amyloid fibril formation. The Journal of Biological Chemistry 280:7800-7807. pdf file
  8. Maity, H., M. Maity, M.M.G. Krishna, L. Mayne, and S.W. Englander (2005) Protein folding: The stepwise assembly of foldon units. Proceedings of the National Academy of Sciences 102:4741-4746. pdf file
  9. Krishna, M.M.G. and S.W. Englander (2005) The N-terminal to C-terminal motif in protein folding and function. Proceedings of the National Academy of Sciences 102:1053-1058. pdf file
  10. Krishna, M.M.G., Y. Lin, and S.W. Englander (2004) Protein misfolding: optional barriers, misfolded intermediates, and pathway heterogeneity. Journal of Molecular Biology 343:1095-1109. pdf file
  11. Maity, H., M. Maity, and S.W. Englander (2004) How cytochrome c folds, and why: submolecular foldon units and their stepwise sequential stabilization. Journal of Molecular Biology 343:223-233. pdf file
  12. Krishna, M.M.G., L. Hoang, Y. Lin, and S.W. Englander (2004) Hydrogen exchange methods to study protein folding. Methods 34:51-64. pdf file
  13. Krishna, M.M.G., Y. Lin, L. Mayne, and S.W. Englander (2003) Intimate view of a kinetic protein folding intermediate: Residue-resolved structure, interactions, stability, folding and unfolding rates, homogeneity. Journal of Molecular Biology 334:501-513. pdf file
  14. Liu, W., J. Rumbley, S.W. Englander, and A.J. Wand (2003) Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c. Protein Science 12:2104-2108. pdf file
  15. Hoang, L., H. Maity, M.M.G. Krishna, Y. Lin, and S.W. Englander (2003) Folding units govern the cytochrome c alkaline transition. Journal of Molecular Biology 331:37-43. pdf file
  16. Krishna, M.M.G., Y. Lin, J.N. Rumbley, and S.W. Englander (2003) Cooperative omega loops in cytochrome c: Role in folding and function. Journal of Molecular Biology 331:29-36. pdf file
  17. Englander, J.J., C. Del Mar, W. Li, S.W. Englander, J.S. Kim, D.D. Stranz, Y. Hamuro, and V.L. Woods, Jr. (2003) Protein structure change studied by hydrogen-deuterium exchange, functional labeling, and mass spectrometry. Proceedings of the National Academy of Sciences 100:7057-7062. pdf file
  18. Maity, H., W.K. Lim, J.N. Rumbley, and S.W. Englander (2003) Protein hydrogen exchange mechanism: Local fluctuations. Protein Science 12, 153-160. pdf file