The chemistry of sulphur enables a disulphide bond to be transitory—guiding the proper folding of a protein, but not appearing in the native structure.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 12 print issues and online access
$189.00 per year
only $15.75 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
References
Robinson, A.S. & King, J. Nature Struct Biol. 4, 450–455 (1997).
Creighton, T.E. J. Mol. Biol. 113, 275–293 (1977).
Rosenfield, R.E., Jr., Parthasarathy, R. & Dunitz, J.D. J. Am. Chem. Soc. 99, 4860–4862 (1977).
Anfinsen, C.B., Haber, E., Sela, M. & White, F.H., Jr. Proc. Natl. Acad. Sci. USA 47, 1309–1314 (1961).
Anfinsen, C.B. & Haber, E. J. Biol. Chem. 236, 1361–1363 (1961).
Gilbert, H.F. Adv. Enzymol. 63, 69–172 (1990).
Gilbert, H.F. Adv. Enzymol. 251, 8–28 (1995).
Chivers, P.T., Prehoda, K.E. & Raines, R.T. Biochemistry 36, 4061–4066 (1997).
Moore, E.C., Reichard, P. & Thelander, L.J. Biol. Chem. 239, 3445–3452 (1964).
Grauschopf, U. et al. Cell 83, 947–955 (1995).
Flory, P.J. Statistical Mechanics of Chain Molecules (Wiley, New York, NY, 1969).
Peng, Z.Y., Wu, L.C. & Kim, P.S. Biochemistry 34, 3248–3252 (1995).
Lees, W.J. & Whitesides, G.M. J. Org. Chem. 58, 642–647 (1993).
Weissman, J.S. & Kim, P.S. Science 253, 1386–1393 (1991).
Hammond, G.S. J. Am. Chem. Soc. 77, 334–338 (1955).
Matouschek, A. & Fersht, A.R. Proc. Natl. Acad. Sci. USA 90, 7814–7818 (1993).
Matouschek, A., Otzen, D.E., Itzhaki, L.S., Jackson, S.E. & Fersht, A.R. Biochemistry 34, 13656–13662 (1995).
Matthews, J.M. & Fersht, A.R. Biochemistry 34, 6805–6814 (1995).
Reed, A.E., Curtiss, L.A. & Weinhold, F. Chem. Rev. 88, 899–926 (1988).
Hwang, C., Sinskey, A.J. & Lodish, H.F. Science 257, 1496–1502 (1992).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Raines, R. Nature's transitory covalent bond. Nat Struct Mol Biol 4, 424–427 (1997). https://doi.org/10.1038/nsb0697-424
Issue Date:
DOI: https://doi.org/10.1038/nsb0697-424
This article is cited by
-
Approaches for the generation of active papain-like cysteine proteases from inclusion bodies of Escherichia coli
World Journal of Microbiology and Biotechnology (2015)