Maki, K., Cheng, H., Dolgikh, D. A. & Roder, H. Folding kinetics of staphylococcal nuclease studied by tryptophan engineering and rapid mixing methods. J. Mol. Biol. 368:244-55, 2007.
Abel, C. J., Goldbeck, R. A., Latypov, R. F., Roder, H. & Kliger, D. S. Conformational equilibration time of unfolded protein chains and the folding speed limit. Biochemistry 46:4090-9, 2007.
Riley, P. W., Cheng, H., Samuel, D., Roder, H. & Walsh, P. N. Dimer Dissociation and Unfolding Mechanism of Coagulation Factor XI Apple 4 Domain: Spectroscopic and Mutational Analysis. J. Mol. Biol. 367:558-73, 2007.
Roder, H., Maki, K. & Cheng, H. Early events in protein folding explored by rapid mixing methods. Chem Rev 106:1836-61, 2006.
Apetri, A. C., Maki, K., Roder, H. & Surewicz, W. K. Early intermediate in human prion protein folding as evidenced by ultrarapid mixing experiments. J. Am. Chem. Soc. 128:11673-8, 2006.
Latypov, R.F., Cheng, H., Roder, N.A., Zhang, J., Roder, H. Structural characterization of an equilibrium unfolding intermediate in cytochrome c. J. Mol. Biol. 357:1009-1025, 2006.
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., Barker, P.D. Effects of heme on the structure of the denatured state and folding kinetics of cytochrome b(562). J. Mol. Biol. 346:331-344, 2005.
Kurchan, E., Roder, H., Bowler, B.E. Kinetics of loop formation and breakage in the denatured state of iso-1-cytochrome c. J. Mol. Biol. 353:730-743, 2005.
Roder, H., Maki, K., Latypov, R.F., Cheng, H., Shastry, M.C.R. Early events in protein folding explored by rapid mixing methods. In Protein Folding Handbook, Part I, edited by J. Buchner, T. Kiefhaber. Wiley-VCH, Weinheim, pp.491-535, 2005.
Hensley, H., Chang, W-C.L., Clapper, M.L. Detection and volume determination of colonic tumors in Min mice by magnetic resonance micro-imaging. Magn. Reson. Med. 52:524-529, 2004.
Maki, K., Cheng, H., Dolgikh, D.A., Shastry, M.C.R., Roder, H. Early events during folding of wild type staphylococcal nuclease and a single-tryptophan variant studied by ultrarapid mixing. J. Mol. Biol. 338:383-400, 2004.
Pabit, S.A., Roder, H., Hagen, S.J. Internal friction controls the speed of protein folding from a compact configuration. Biochemistry 43:12532-12538, 2004.
Roder, H. Stepwise helix formation and chain compaction during protein folding. Proc. Natl. Acad. Sci. USA 101:1793-1794, 2004.
Roder, H., Maki, K., Cheng, H., Shastry, M.C.R. Rapid mixing methods for exploring the kinetics of protein folding. Methods 34:15-27, 2004.
Welker, E., Maki, K., Shastry, M.C., Juminaga, D., Bhat, R., Scheraga, H.A., Roder, H. Ultrarapid mixing experiments shed new light on the characteristics of the initial conformational ensemble during the folding of ribonuclease A. Proc. Natl. Acad. Sci. USA 101:17681-17686, 2004.
Gianni, S., Travaglini-Allocatelli, C., Cutruzzola, F., Brunori, M., Shastry, M.C., Roder, H. Parallel pathways in cytochrome c(551) folding. J. Mol. Biol. 330:1145-1152, 2003.
Kuwata, K., Matumoto, T., Cheng, H., Nagayama, K., James, T.L., Roder, H. NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126. Proc. Natl. Acad. Sci. USA 100:14790-14795, 2003.
Zhang, Y.Z., Cheng, H., Gould, K.L., Golemis, E.A., Roder, H. Structure, Stability, and Function of hDim1 Investigated by NMR, Circular Dichroism, and Mutational Analysis. Biochemistry 42:9609-9618, 2003.
Zhu, Y., Alonso, D.O., Maki, K., Huang, C.Y., Lahr, S.J., Daggett, V., Roder, H., DeGrado, W.F., Gai, F. Ultrafast folding of a3D: A de novo designed three-helix bundle protein. Proc. Natl. Acad. Sci. USA 100:15486-15491, 2003.
Abdulaev, Z.K., Bodrova, M.E., Chernyak, B.V., Dolgikh, D.A., Kluck, R.M., Pareversev, M.O., Arseniev, A.S., Efremov, R.G., Kirpichnikov, M.P., Mokhova, E.N., Newmeyer, D.D., Roder, H., Skulachev, V.P. A cytochrome c mutant of high electron transfer and antioxidant activities but devoid of apoptogenic effect. Biochem. J. 362:749-754, 2002.
Hagen, S.J., Latypov, R.F., Dolgikh, D.A., Roder, H. Rapid intrachain binding of His-26 and His-33 to heme in unfolded ferrocytochrome c. Biochemistry 41:1372-1380, 2002.
Teilum, K., Maki, K., Kragelund, B.B., Poulsen, F.M., Roder, H. Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing. Proc. Natl. Acad. Sci. USA 99:9807-12, 2002.
Yi, J., Cheng, H., Andrake, M.D., Dunbrack, R.L. Jr., Roder, H., Skalka, A.M. Mapping the epitope of an inhibitory monoclonal antibody to the C-terminal DNA-binding domain of HIV-1 integrase. J. Biol. Chem. 277:12164-74, 2002.