S. Walter Englander, Ph.D

faculty photo
Emeritus Professor of Biochemistry and Biophysics
Department: Biochemistry and Biophysics
Graduate Group Affiliations

Contact information
1005-09 Stellar-Chance Laboratories
422 Curie Blvd.
Philadelphia, PA 19104
Office: (215) 898-4509
Fax: (215) 898-2415
Lab: (215) 898-4509
B.S. (Physics/Math)
University of Maryland, 1951.
M.S. (Biophysics)
University of Pittsburgh, 1953.
Ph.D. (Biophysics)
University of Pittsburgh, 1959.
Postdoc (Protein Chem)
National Inst. of Health, 1960.
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Description of Research Expertise

Dr. Englander's laboratory is interested in macromolecular structure, dynamics, and function and has developed the use of hydrogen exchange (HX) approaches in protein and nucleic acid studies. Many hydrogens in proteins and nucleic acids are in continual exchange with the hydrogens in solvent water. These can provide literally hundreds of probe points that are sensitive to structure, structure change, internal dynamics, energy, and functional interactions at identifiable positions throughout a macromolecule. Work in this lab has explained the chemistry of protein and nucleic acid HX processes and has formulated the physical models that appear to explain the ways in which internal motions in proteins and nucleic acids determine the HX rates of their individual protons. 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 bonding interactions, structure change, etc.

Methods in use include the range of protein biophysical techniques including 2D NMR and mutational analysis. The lab has in recent years produced a coherent explanation for how proteins fold. Present work is directed at testing and enlarging this model.

Selected Publications

Milne JS., Xu Y., Mayne LC., Englander SW.: Experimental study of the protein folding landscape: unfolding reactions in cytochrome c. Journal of Molecular Biology 290(3): 811-22, Jul 16 1999.

Shtilerman M., Lorimer GH., Englander SW.: Chaperonin function: folding by forced unfolding. Science 284(5415): 822-5, Apr 30 1999.

Xu Y., Mayne L., Englander SW.: Evidence for an unfolding and refolding pathway in cytochrome c. Nature Structural Biology 5(9): 774-8, Sep 1998.

Englander SW.: Native-state HX. [letter; comment] Trends in Biochemical Sciences 23(10): 378; discussion 379-81, Oct 1998.

Englander JJ., Rumbley JN., Englander SW.: Signal transmission between subunits in the hemoglobin T-state. Journal of Molecular Biology 284(5): 1707-16, Dec 18 1998.

Englander JJ., Louie G., McKinnie RE., Englander SW.: Energetic components of the allosteric machinery in hemoglobin measured by hydrogen exchange. Journal of Molecular Biology 284(5): 1695-706, Dec 18 1998.

Qi PX., Sosnick TR., Englander SW.: The burst phase in ribonuclease A folding and solvent dependence of the unfolded state. [see comments] Nature Structural Biology 5(10): 882-4, Oct 1998.

Milne JS., Mayne L., Roder H., Wand AJ., Englander SW.: Determinants of protein hydrogen exchange studied in equine cytochrome c. Protein Science 7(3): 739-45, Mar 1998.

Englander, S. W., Sosnick, T. R., Mayne, L. C., Shtilerman, M., Qi, P. X. & Bai, Y: Fast and slow folding in cytochrome c. Accts. Chem. Res 31: 737-744, 1998.

Englander, J. J., Louie, G., McKinnie, R. E. , Englander, S. W: Energetic components of the allosteric machinery In hemoglobin measured by hydrogen exchange. J. Mol. Biol 284: 1695-1706, 1998.

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Last updated: 12/07/2012
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