HEINRICH RODER lab
Protein folding, dynamics and function

Job Opportunities

Postdoctoral positions are available in the Roder group to study protein structure and folding using NMR, optical spectroscopy and other biophysical methods. Candidates should have a Ph.D. and research experience in biophysics and/or biochemistry. Possible projects include: 1) kinetic studies of early protein folding events in model proteins, such as staph. nuclease, cytochrome c and apomyoglobin, using ultrafast mixing in combination with optical probes and/or NMR-detected H/D exchange; 2) studies of molecular interactions, dynamics and folding of blood coagulation factor XI and cell signaling proteins containing PDZ domains using NMR and other spectroscopic methods. The Fox Chase Cancer Center, a non-profit research center located at the outskirts of Philadelphia, provides a stimulating and interactive research environment. Please send curriculum vitae and three references to: Heinrich Roder, Ph.D., Fox Chase Cancer Center, Philadelphia, PA 19111; e-mail: Roder@fccc.edu.

Recent Papers

D. Samuel, H. Cheng, P. W. Riley, A. A. Canutescu, C. Nagaswami, J. W. Weisel, Z. Bu, P. N. Walsh, and H. Roder (2007) Solution structure of the A4 domain of factor XI sheds light on the mechanism of zymogen activation. Proc. Natl. Acad. Sci. USA, 104:15693-98. (pdf)

Bender, G.M., Lehmann, A., Zou, H., Cheng, H., Fry, H.C., Engel, D., Therien, M.J., Blasie, J.K., Roder, H., Saven, J.G., and Degrado, W.F. (2007). De Novo Design of a Single-Chain Diphenylporphyrin Metalloprotein. J. Am. Chem. Soc. 129:10732-10740. (pdf)

Maki, K., Cheng, H., Dolgikh, D. A. & Roder, H. (2007) Folding kinetics of staphylococcal nuclease studied by tryptophan engineering and rapid mixing methods. J. Mol. Biol., 368:244-255. (pdf)

Abel, C.J., Goldbeck, R.A., Latypov, R.F., Roder, H., & Kliger, D.S. (2007) Conformational equilibration time of unfolded protein chains and the folding speed limit. Biochemistry, 46:4090-4099. (pdf)

Riley, P. W., Cheng, H., Samuel, D., Roder, H. & Walsh, P. N. (2007). Dimer Dissociation and Unfolding Mechanism of Coagulation Factor XI Apple 4 Domain: Spectroscopic and Mutational Analysis. J. Mol. Biol. 367:558-573. (pdf)

Apetri, A. C., Maki, K., Roder, H. & Surewicz, W. K. (2006) Early intermediate in human prion protein folding as evidenced by ultrarapid mixing experiments. J. Am. Chem. Soc. 128:11673-8. (pdf)

Roder, H., Maki,K. & Cheng, H. (2006). Early events in protein folding explored by rapid mixing methods. Chem. Rev. 106(5): 1836-1861. (pdf)

Latypov, R. F., Cheng, H., Roder, N. A., Zhang, J. & Roder, H. (2006). Structural Characterization of an Equilibrium Unfolding Intermediate in Cytochrome c. J. Mol. Biol. 357:1009-1025 (pdf)

Kurchan, E., Roder, H. & Bowler, B.E. (2005) Kinetics of Loop Formation and Breakage in the Denatured State of Iso-1-cytochrome c. J. Mol. Biol. 353:730-43. (pdf)

Roder, H., Maki, K., Latypov, R. F., Cheng, H. & Shastry, M. C. R. (2005). Early events in protein folding explored by rapid mixing methods. In Protein Foldign Handbook, Vol. Part I, pp. 491-535. Wiley-VCH, Weinheim. (pdf)

Garcia, P., Bruix, M., Rico, M., Ciofi-Baffoni, S., Banci, L., Ramachandra Shastry, M. C., Roder, H., de Lumley Woodyear, T., Johnson, C. M., Fersht, A. R., et al. (2005). Effects of Heme on the Structure of the Denatured State and Folding Kinetics of Cytochrome b(562). J. Mol. Biol. 346:331-344. (pdf)