Archives of Englander Lab Publications

 

  1. Mallela M. G. Krishna, Haripada Maity, Jon N. Rumbley, Yan Lin, S. Walter Englander (2006). Order of steps in the cytochrome c folding pathway: Evidence for a sequential stabilization mechanism. Journal of Molecular Biology 359, 1410-1419.
  2. Haripada Maity, Jon N. Rumbley, S. Walter Englander (2006). Functional role of a protein foldon – An W-loop foldon controls the alkaline transition in ferricytochrome c. Proteins: Structure, Function, and Bioinformatics 63, 349-355.
  3. Charyl Del Mar, Eric A. Greenbaum, Leland Mayne, S. Walter Englander, and Virgil L. Woods, Jr. (2005). Structure and properties of a-synuclein and other amyloids determined at the amino acid level. Proceedings of the National Academy of Sciences 102, 15477-15482.
  4. Eric A. Greenbaum, Charles L. Graves, Amanda J. Mishizen-Eberz, Michael A. Lupoli, David R. Lynch, S. Walter Englander, Paul H. Axelsen, and Benoit I. Giasson (2005). The E46K mutation in a-synuclein increases amyloid fibril formation. The Journal of Biological Chemistry 280, 7800-7807.
  5. Haripada Maity, Mita Maity, Mallela M. G. Krishna, Leland Mayne, and S. Walter Englander (2005). Protein folding: The stepwise assembly of foldon units. Proceedings of the National Academy of Sciences 102, 4741-4746.
  6. Mallela M. G. Krishna, and S. Walter Englander (2005). The N-terminal to C-terminal motif in protein folding and function. Proceedings of the National Academy of Sciences 102, 1053-1058.
  7. Mallela M. G. Krishna, Yan Lin, and S. Walter Englander (2004). Protein misfolding: optional barriers, misfolded intermediates, and pathway heterogeneity. Journal of Molecular Biology 343, 1095-1109.
  8. Haripada Maity, Mita Maity, and S. Walter Englander (2004). How cytochrome c folds, and why: submolecular foldon units and their stepwise sequential stabilization. Journal of Molecular Biology 343, 223-233.
  9. Mallela M. G. Krishna, Linh Hoang, Yan Lin, and S. Walter Englander (2004). Hydrogen exchange methods to study protein folding. Methods 34, 51-64.
  10. Mallela M. G. Krishna, Yan Lin, Leland Mayne, and S. Walter 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.
  11. Weixia Liu, Jon Rumbley, S. Walter Englander, and A. Joshua Wand (2003). Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c. Protein Science 12, 2104-2108.
  12. Linh Hoang, Haripada Maity, Mallela M. G. Krishna, Yan Lin, and S. Walter Englander (2003). Folding Units Govern the Cytochrome c Alkaline Transition. Journal of Molecular Biology 331, 37-43.
  13. Mallela M. G. Krishna, Yan Lin, Jon N. Rumbley, and S. Walter Englander (2003). Cooperative omega loops in Cytochrome c: Role in folding and function. Journal of Molecular Biology 331, 29-36.
  14. Joan J. Englander, Charyl Del Mar, Will Li, S. Walter Englander, Jack S. Kim, David D. Stranz, Yoshitomo Hamuro, and Virgil 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.
  15. Haripada Maity, Woon Ki Lim, Jon N. Rumbley, and S. Walter Englander (2003). Protein hydrogen exchange mechanism: Local fluctuations. Protein Science 12, 153-160.
  16. S. Walter Englander, Leland Mayne, and Jon N. Rumbley (2002). Submolecular cooperativity produces multi-state protein unfolding and refolding. Biophysical Chemistry 101-102, 57-65.
  17. Jon N. Rumbley, Linh Hoang, and S. Walter Englander (2002). Recombinant equine Cytochrome c in Escherichia coli: High-level expression, characterization, and folding and assembly mutants. Biochemistry 41, 13894-13901.
  18. Bryan A. Krantz, Leland Mayne, Jon Rumbley, S. Walter Englander, and Tobin R. Sosnick (2002). Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding. Journal of Molecular Biology 324, 359-371.
  19. Linh Hoang, Sabrina Bedard, Mallela M. G. Krishna, Yan Lin, and S. Walter Englander (2002). Cytochrome c folding pathway: Kinetic hydrogen exchange. Proceedings of the National Academy of Sciences 99, 12173-12178.
  20. Umamaheswar Duvvuri, Ari D. Goldberg, James K. Kranz, Linh Hoang, Ravinder Reddy, Felix W. Wehrli, A. Joshua Wand, S. W. Englander, and John S. Leigh (2001). Water magnetic relaxation dispersion in biological systems: The contribution of proton exchange and implications for the noninvasive detection of cartilage degradation. Proceedings of the National Academy of Sciences 98 12479-12484.
  21. Jon Rumbley, Linh Hoang, Leland Mayne, and S. Walter Englander (2001). An amino acid code for protein folding. Proceedings of the National Academy of Sciences 98, 105-112.
  22. S. Walter Englander & Mallela M. G. Krishna (2001). Hydrogen Exchange. Nature Structural Biology 8, 1-2.
  23. S. Walter Englander & Reuben Hiller (2001). Dynamics and thermodynamics of hyperthermophili proteins by hydrogen exchange. Methods in Enzymology 334: 342-350.
  24. Leland Mayne & S. Walter Englander (2000). Two-state vs. multistate protein unfolding studied by optical melting and hydrogen exchange. Protein Science 9, 1873-1877.
  25. S. Walter Englander (2000). Protein folding intermediates and pathways studied by hydrogen exchange. Annual Review of Biophysics and Biomolecular Structure 29, 213-38.
  26. John S. Milne, Yujia Xu, Leland C. Mayne, and S. Walter Englander (1999). Experimental study of the protein folding landscape: Unfolding reactions in Cytochrome c. Journal of Molecular Biology, 290, 811-822.
  27. Mark Shtilerman, George H. Lorimer, and S. Walter Englander (1999). Chaperonin function: Folding by forced unfolding. Science 284, 822-825.
  28. Joan J. Englander, Jon N. Rumbley, and S. Walter Englander (1998). Signal transmission between subunits in the hemoglobin T-state. Journal of Molecular Biology 284, 1707-1716.
  29. Joan J. Englander, Godfrey Louie, Russell E. McKinnie, and S. Walter Englander (1998). Energetic components of the allosteric machinaery in hemoglobin measured by hydrogen exchange. Journal of Molecular Biology 284, 1695-1706.
  30. S. Walter Englander, Tobin R. Sosnick, Leland Mayne, Mark Shtilerman, Phoebe X. Qi, and Yawen Bai (1998). Fast and slow folding in Cytochrome c. Accounts of Chemical Research 31, 737-744.
  31. Phoebe X. Qi, Tobin R. Sosnick and S. Walter Englander (1998). The burst phase in Ribonuclease A folding and solvent dependence of the unfolded state. Nature Structural Biology 5 882-884.
  32. Yujia Xu, Leland Mayne, and S. Walter Englander (1998). Evidence for an unfolding and refolding pathway in cytochrome c. Nature Structural Biology 5, 774-778.
  33. John S. Milne, Leland Mayne, H. Roder, A. Joshua Wand, and S. Walter Englaner (1998). Determinants of protein hydrogen exchange studied in equine Cytochrome c. Protein Science 7, 739-745.
  34. S. Walter Englander (1998). Native-state HX. Trends in Biochemical Sciences 23: 378.
  35. Leland Mayne, S. Walter Englander, Rong Qiu, Jianxin Yang, Youxiang Gong, Erik J. Spek, and Neville R. Kallenbach (1998). Stabilizing effect of a multiple salt bridge in a prenucleated peptide. Journal of The American Chemical Society 120, 10643-10645.
  36. Tobin R. Sosnick, Mark D. Shtilerman, Leland Mayne, and S. Walter Englander (1997). Ultrafast signals in protein folding and the polypeptide contracted State. Proceedings of the National Academy of Sciences 94 8545-8550.
  37. Reuben Hiller, Zhi H. Zhou, Michael W. W. Adams, and S. Walter Englander (1997). Stability and Dynamics in a hyperthermophilic protein with melting temperature close to 200oC. Proceedings of the National Academy of Sciences 94 11329-11332.
  38. S. W. Englander, L. Mayne, Y. Bai, and T. R. Sosnick (1997). Hydrogen exchange: The modern legacy of Linderstrøm-Lang. Protein Science 6, 1101-1109.
  39. Tobin R. Sosnick, Sharon Jackson, Rosemarie R. Wilk, S. Walter Englander, and William F. DeGrado (1996). The role of helix formation in the folding of a fully a-helical coiled coil. Proteins: Structure, Function, and Genetics 24: 427-432.
  40. Tobin R. Sosnick, Leland Mayne, and S. Walter Englander (1996). Molecular collapse: The rate-limiting step in two-state cytochrome c folding. Proteins: Structure, Function, and Genetics 24, 413-426.
  41. S. Walter Englander, Tobin R. Sosnick, Joan J. Englander, and Leland Mayne (1996). Mechanisms and uses of hydrogen exchange. Current Opinion in Structural Biology 6: 18-23.
  42. Yawen Bai and S. Walter Englander (1996). Future directions in folding: The multi-state nature of protein structure. Proteins: Structure, Function, and Genetics 24: 145-151.
  43. Michael E. Rodgers, Joan J. Englander, S. Walter Englander, and William F. Harrington (1996). Measurement of protein structure change in active muscle by hydrogen-tritium exchange. Biophysical Chemistry 59: 221-230.
  44. A. Joshua Wand & S. Walter Englander (1996). Protein complexes studied by NMR spectroscopy. Current Opinion in Biotechnology 7, 403-408.
  45. Louis Carlacci and S. Walter Englander (1996). Loop problem in proteins: Developments on the Monte Carlo simulated annealing approach. Journal of Computational Chemistry 17: 1002-1012.
  46. Yawen Bai, Tobin R. Sosnick, Leland Mayne, and S. Walter Englander (1995). Protein folding intermediates: Native-state hydrogen exchange. Science 269 192-197.
  47. Yawen Bai, John S. Milne, Leland Mayne, and S. Walter Englander (1994). Protein stability parameters measured by hydrogen exchange. Proteins: Structure, Function, and Genetics 20: 4-14.
  48. Yawen Bai and S. Walter Englander (1994). Hydrogen bond strength and b-sheet propensities: The role of a side chain blocking effect. Proteins: Structure, Function, and Genetics 18, 262-266.
  49. Gregory P. Connelly, Yawen Bai, Mei-Fen Jeng, and S. Walter Englander (1993). Isotope effects in peptide group hydrogen exchange. Proteins: Structure, Function, and Genetics 17, 87-92.
  50. Yawen Bai, John S. Milne, Leland Mayne, and S. Walter Englander (1993). Primary structure effects on peptide group hydrogen exchange. Proteins: Structure, Function, and Genetics 17, 75-86.
  51. Louis Carlacci and S. Walter Englander (1993). The loop problem in proteins: A Monte Carlo simulated annealing approach. Biopolymers 33: 1271-1286.
  52. Dorothy B. Calhoun, Jane M. Vanderkooi, Gary R. Holtom, and S. Walter Englander (1986). Protein fluorescence quenching by small molecules: Protein penetration versus solvent exposure. Proteins: Structure, Function, and Genetics 1:109-115.
  53. R. S. Preisler, C. Mandal, S. W. Englander, and N. R. Kallenbach (1984). Premelting and the hydrogen-exchange open state in synthetic RNA duplexes. Biopolymers 23: 2099-2125.
  54. S. W. Englander and A. Poulsen (1969). Hydrogen-tritium exchange of the random chain polypeptide. Biopolymers 7: 379-393.

 

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