Direct NMR observation of a transient folding intermediate provides new evidence for the importance of molten globules as general intermediates in protein folding.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 12 print issues and online access
$259.00 per year
only $21.58 per issue
Buy this article
- Purchase on SpringerLink
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
References
Kim, P.S. & Baldwin, R.L. A. Rev. Biochem. 59, 631–660 (1990).
Matthews, C.R. A. Rev. Biochem. 62, 653–683 (1993).
Evans, P.A. & Radford, S.E. Curr. Opin. Struct. Biol. 4, 100–106 (1994).
Roder, H. & Elöve, G.A. In Mechanisms of Protein Folding: Frontiers in Molecular Biology. (Ed. Pain, R.H.), 26–55 (Oxford University Press, New York; 1994).
Kuwajima, K. Proteins 6, 87 (1989).
Ptitsyn, O.B. In Protein Folding. (Ed. Creighton, T.E.), 243–300 (W. H. Freeman & Co., New York; 1992).
Ptitsyn, O.B., Pain, R.H., Semisotnov, G.V., Zerovnik, E. & Razgulyaev, O.I. FEBS Lett. 262, 20 (1990).
Balbach, J., Forge, V., van Nuland, N.A.J., Winder, S.L., Hore, P.J. & Dobson, C.M. Nature Struct. Biology 2, 866–870 (1995).
Matthews, C.R. Meth. Enzymol. 154, 498–511 (1987).
Matouschek, A., Kellis, J.T., Jr., Serrano, L., Bycroft, M. & Fersht, A.R. Nature 346, 440–445 (1990).
Fersht, A.R. FEBS Lett. 325, 5–16 (1993).
Wüthrich, K. NMR of Proteins and Nucleic Acids. (John Wiley & Sons, New York; 1986).
Roder, H. Meth. Enzymol. 176, 446–473 (1989).
Roder, H. & Wüthrich, K. Proteins 1, 34–42 (1986).
Udgaonkar, J.B. & Baldwin, R.L. Nature 335, 694–699 (1988).
Roder, H., Elöve, G.A. & Englander, S.W. Nature 335, 700–704 (1988).
Udgaonkar, J.B. & Baldwin, R.L. Proc. natn. Acad. Sci. U.S.A. 87, 8197–8201 (1990).
Elöve, G.A. & Roder, H. ACS Symp. Ser. 470, 50–63 (1991).
Baldwin, R.L. & Roder, H. Curr. Biol. 1, 218–220 (1991).
Englander, S.W. & Mayne, L. A. Rev. Biophys. Biomol. Struct. 21, 243–265 (1992).
Baldwin, R.L. Curr. Opin. Struct. Biol. 3, 84–91 (1993).
Blum, A.D., Smallcombe, S.H. & Baldwin, R.L. J. molec. Biol. 118, 305–316 (1978).
Adler, M. & Scheraga, H.A. Biochemistry 27, 2471–2480 (1988).
Kautz, R.A. & Fox, R.O. Protein Sci. 2, 851–858 (1993).
Frieden, C., Hoeltzli, S.D. & Ropson, I.J. Protein Sci. 2, 2007–2014 (1993).
Hoeltzli, S.D., Ropson, I.J. & Frieden, C. In Techniques in Protein Chemistry V. 455–465 (Academic Press, San Diego; 1994).
Marion, D., Ikura, M., Tschudin, R. & Bax, A. J. Magn. Reson. 85, 393–399 (1989).
Ruiz-Cabello, J., Vuister, G.W., Moonen, C.T.W., van Gelderen, P., Cohen, J.S. & van Zijl, P.C.M. J. Magn. Reson. 100, 282–302 (1992).
Kuwajima, K., Mitani, M. & Sugai, S. J. molec. Biol. 206, 547–561 (1989).
Ikeguchi, M., Kuwajima, K., Mitani, M. & Sugai, S. Biochemistry 25, 6965–6972 (1986).
Jennings, P.A. & Wright, P.E. Science 262, 892–895 (1993).
Hughson, F.M., Wright, P.E. & Baldwin, R.L. Science 249, 1544–1548 (1990).
Hughson, F.M., Barrick, D. & Baldwin, R.L. Biochemistry 30, 4113–4118 (1991).
Baum, J., Dobson, C.M., Evans, P.A. & Hanley, C. Biochemistry 28, 7 (1989).
Chyan, C.L., Wormald, C., Dobson, C.M., Evans, P.A. & Baum, J. Biochemistry 32, 5681–5691 (1993).
Schulman, B.A., Redfield, C., Peng, Z.Y., Dobson, C.M. & Kim, P.S. J. molec. Biol. in the press.
Ban, N. & Dobson, C. Nature struct. Biol. 2, 871–875 (1995).
Jeng, M.-F., Englander, S.W., Elöve, G.A., Wand, A.J. & Roder, H. Biochemistry 29, 10433–10437 (1990).
Marmorino, J.L. & Pielak, G.J. Biochemistry 34, 3140–3143 (1995).
Dobson, C.M. Current Biology 4, 636–640 (1994).
Alexandrescu, A.T., Evans, P.A., Pitkeatly, M., Baum, J. & Dobson, C.M. Biochemistry 32, 1707–1718 (1993).
Ewbank, J.J. & Creighton, T.E. Nature 350, 518–520 (1991).
Peng, Z.-y. & Kim, P.S. Biochemistry 33, 2136–2141 (1994).
Ewbank, J.J. & Creighton, T.E. Biochemistry 32, 3677–3693 (1993).
Wu, L.C., Peng, Z.-y. & Kim, P.S. Nature struct. Biology 2, 281–286 (1995).
Sali, A., Shaknovich, E. & Karplus, M. Nature 369, 248–251 (1994).
Gutin, A.M., Abkevich, V.I. & Shakhnovich, E.I. Biochemistry 34, 3066–3076 (1995).
Acharya, K.R., Ren, J., Stuart, D.I. & Phillips, D.C. J. molec. Biol. 221, 571–581 (1991).
Wolynes, P.G., Onuchic, J.N. & Thirumalai, D. Science 267, 1619–1620 (1995).
Sosnick, T.R., Mayne, L., Hiller, R. & Englander, S.W. Nature struct. Biology 1, 149–156 (1994).
Schmid, F.X. In Protein Folding. (Ed. Creighton, T.E.) 197–241 (W.H. Freeman & Co., New York; 1992).
Odefey, C., Mayr, L.M. & Schmid, F.X. J. molec. Biol. 245, 69–78 (1995).
Creighton, T.E. Biochem. J. 270, 1–16 (1990).
Weissman, J.S. & Kim, P.S. Proc. natn. Acad. Sci. U.S.A. 89, 9900–9904 (1992).
Elöve, G.A., Bhuyan, A.K. & Roder, H. Biochemistry 33, 6925–6935 (1994).
Wu, L., Laub, P.B., Elöve, G.A., Carey, J. & Roder, H. Biochemistry 32, 10271–10276 (1993).
Dobson, C.M. Nature struct. Biology 2, 513–517 (1995).
Jackson, S.E. & Fersht, A.R. Biochemistry 30, 10428–10435 (1991).
Alexander, P., Orban, J. & Bryan, P. Biochemistry 31, 7243–7248 (1992).
Viguera, A.R., Martúnez, J.C., Filimonov, V.V., Mateo, P.L. & Serrano, L. Biochemistry 33, 2142–2150 (1994).
Kragelund, B.B., Robinson, C.V., Knudsen, J., Dobson, C.M. & Poulsen, F.M. Biochemistry 34, 7217–7224 (1995).
Schindler, T., Herrler, M., Marahiel, M.A. & Schmid, F.X. Nature atruct. Biology 2, 663–673 (1995).
Khorasanizadeh, S., Peters, I.D., Butt, T.R. & Roder, H. Biochemistry 32, 7054–7063 (1993).
Houry, W.A., Rothwarf, D.M. & Scheraga, H.A. Biochemistry 33, 2516–2530 (1994).
Jones, C.M. et al. Proc. natn. Acad. Sci. U.S.A. 90, 11860–11864 (1993).
Regenfuss, P., Clegg, R.M., Fulwyler, M.J., Barrantes, F.J. & Jovin, T.M. Rev. Sci. Instrum. 56, 283–290 (1985).
Kraulis, P.J. J. Appl. Cryst. 24, 946–950 (1991).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Roder, H. Watching protein folding unfold. Nat Struct Mol Biol 2, 817–820 (1995). https://doi.org/10.1038/nsb1095-817
Published:
Issue date:
DOI: https://doi.org/10.1038/nsb1095-817
This article is cited by
-
Speeding along the protein folding highway, are we reading the signs correctly?
Nature Structural Biology (1998)
-
Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues
Nature Structural Biology (1996)