The Folding Pathway of Disulfide Containing Proteins
197
The structures of scrambled hirudin and TAP imply that their 1- and 2disulfide intermediates may be equally heterogeneous. The presence of significant amount of scrambled species along the folding pathway of hirudin, TAP, PCI
and EGF also indicate that they could not be simply dismissed as by-product or
abortive structures of mis-folding. Indeed, scrambled species have also been
observed during the productive folding of ribonuclease A (Creighton, 1979) and
pro-BPTI (Weissmann & Kim, 1992b) that involved no denaturants.
5
Acknowledgements
I would like to acknowledge the collaboration with Dr. F. X. Aviles and Dr. P. H.
Lai in the analysis of folding mechanism of potato carboxypeptidase inhibitor
and human epidermal growth factor.
References
Autuch, W., GUntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H., and WUthrich, K. (1994) FEBS
Lett. 352, 251-257.
Baldwin, R. 1. (1989) Trends Biochem. Sci. 14, 292-294.
Boernsen, K. 0., Schaer, M., and Widmer, M. (1990) Chimia 44, 412-416.
Chang, J.-Y. (1993) J. BioI. Chem. 268,4043-4049.
Chang, J.-Y. (1994) Biochem. J. 300, 643-650.
Chang, J.-Y. (1995) J. BioI. Chem. 270, 25661-25666.
Chang, J.-Y. (1996) Biochemistry 35,11702-11709.
Chang, J.-Y. and Knecht, R. (1991) Anal. Biochem. 197,52-58. J. Bioi
Chang, J.-Y., Canals, F., Schindler, P., Querol, E., and Aviles, F. X. (1994). Chern. 269, 22087-22094.
Chang, J.-Y., Schindler, P., Ramseier, u., and Lai, P.-H. (1995) J. Bioi. Chem. 270, 9207-9216.
Chatrenet, B., and Chang, J.-Y. (1993) J. BioI. Chem. 268, 20988-20996.
Creighton, T. E. (1978) Prog. Biophys. Mol. BioI. 33, 231-297.
Creighton, T. E. (1979) J. Mol. BioI. 129,411-431.
Creighton, T. E. (1986) Methods Enzymol. 131,83-106.
Creighton, T. E. (1990) Biochem. J. 270,1-16.
Creighton, T. E. (1992) Science 256, 111-112.
Jennings, P. A., and Wright, P. E. (1993) Science 262, 892-896.
Kim, P. S., and Baldwin, R. 1. (1990) Annu. Rev. Biochem. 59, 631-660.
Lim-Wilby, M. S. 1., Hallenga, K., De Maeyer, M., Lasters, 1., Vlasuk, G. P., and Brunck, T. K. (1995)
Protein Sci. 4, 178-186.
.
Lyles, M. M., and Gilbert, H. F. (1991) Biochemistry 30, 613-619.
Matthews, C. R. (1993) Annu. Rev. Biochem. 62, 653-683.
Richards, F. M. (1991) Sci. Am. 34-41.
Roder, H., Elove, G., Englander, S. W. (1988) Nature 335,700-704.
Sexena V. P., and Wetlaufer, D. B. (1970) Biochemistry 9,5015-5023.
Udgaonkar, J. B., and Baldwin, R. 1. (1988) Nature 335, 694-699.
Weissman, J. S., and Kim, P. S. (1991) Science 253,1386-1393.
Weissman, J. S., and Kim, P. S. (1992a) Science 256,112-114.
Weissman, J. S., and Kim, P. S. (1992b) Cell 71, 841-851.
197
The structures of scrambled hirudin and TAP imply that their 1- and 2disulfide intermediates may be equally heterogeneous. The presence of significant amount of scrambled species along the folding pathway of hirudin, TAP, PCI
and EGF also indicate that they could not be simply dismissed as by-product or
abortive structures of mis-folding. Indeed, scrambled species have also been
observed during the productive folding of ribonuclease A (Creighton, 1979) and
pro-BPTI (Weissmann & Kim, 1992b) that involved no denaturants.
5
Acknowledgements
I would like to acknowledge the collaboration with Dr. F. X. Aviles and Dr. P. H.
Lai in the analysis of folding mechanism of potato carboxypeptidase inhibitor
and human epidermal growth factor.
References
Autuch, W., GUntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H., and WUthrich, K. (1994) FEBS
Lett. 352, 251-257.
Baldwin, R. 1. (1989) Trends Biochem. Sci. 14, 292-294.
Boernsen, K. 0., Schaer, M., and Widmer, M. (1990) Chimia 44, 412-416.
Chang, J.-Y. (1993) J. BioI. Chem. 268,4043-4049.
Chang, J.-Y. (1994) Biochem. J. 300, 643-650.
Chang, J.-Y. (1995) J. BioI. Chem. 270, 25661-25666.
Chang, J.-Y. (1996) Biochemistry 35,11702-11709.
Chang, J.-Y. and Knecht, R. (1991) Anal. Biochem. 197,52-58. J. Bioi
Chang, J.-Y., Canals, F., Schindler, P., Querol, E., and Aviles, F. X. (1994). Chern. 269, 22087-22094.
Chang, J.-Y., Schindler, P., Ramseier, u., and Lai, P.-H. (1995) J. Bioi. Chem. 270, 9207-9216.
Chatrenet, B., and Chang, J.-Y. (1993) J. BioI. Chem. 268, 20988-20996.
Creighton, T. E. (1978) Prog. Biophys. Mol. BioI. 33, 231-297.
Creighton, T. E. (1979) J. Mol. BioI. 129,411-431.
Creighton, T. E. (1986) Methods Enzymol. 131,83-106.
Creighton, T. E. (1990) Biochem. J. 270,1-16.
Creighton, T. E. (1992) Science 256, 111-112.
Jennings, P. A., and Wright, P. E. (1993) Science 262, 892-896.
Kim, P. S., and Baldwin, R. 1. (1990) Annu. Rev. Biochem. 59, 631-660.
Lim-Wilby, M. S. 1., Hallenga, K., De Maeyer, M., Lasters, 1., Vlasuk, G. P., and Brunck, T. K. (1995)
Protein Sci. 4, 178-186.
.
Lyles, M. M., and Gilbert, H. F. (1991) Biochemistry 30, 613-619.
Matthews, C. R. (1993) Annu. Rev. Biochem. 62, 653-683.
Richards, F. M. (1991) Sci. Am. 34-41.
Roder, H., Elove, G., Englander, S. W. (1988) Nature 335,700-704.
Sexena V. P., and Wetlaufer, D. B. (1970) Biochemistry 9,5015-5023.
Udgaonkar, J. B., and Baldwin, R. 1. (1988) Nature 335, 694-699.
Weissman, J. S., and Kim, P. S. (1991) Science 253,1386-1393.
Weissman, J. S., and Kim, P. S. (1992a) Science 256,112-114.
Weissman, J. S., and Kim, P. S. (1992b) Cell 71, 841-851.