Abstract
Little is known about the mechanism of the transition between native proteins and partially folded intermediates. Complete assignments of 2D 1H–NOESY spectra of CHABII at 5 °C, pH 6.3, 5.5, 4.6 and 4.0, reveal that lowering of pH results in an extensive but gradual disappearance of NOEs, implying a gradual disruption of tight side–chain packing. Moreover, a tertiary packing core is identified at 5 °C and pH 4.0, characterized by persistent long–range NOEs. Thus, we suggest that severe disruption of tight side–chain packing of CHABII can occur at a stage where its secondary structure and tertiary topology remain highly native–like.
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
Similar content being viewed by others
References
Levitt, M., Gerstein, M., Huang, E., Subbiah, S. & Tsai, J. Annu. Rev. Biochem. 66, 549– 579 (1997).
Handel, T.W., Williams, S.A. & De Grado, W.F. Science 261, 879– 885 (1993).
Betz, S.F., Raleigh, D.P. & DeGrado, W.F. Curr. Opin. Struct. Biol. 3, 601–610 (1993).
Noggle, J.H. & Schirmer, R.F. The nuclear Overhauser effect: chemical applications (Academic Press, New York; 1971 ).
Wüthrich, K. NMR of proteins and nucleic acids (John Wiley, New York; 1986).
Dyson, H.J. & Wright, P.E. Nature Struct. Biol. 5, 499–503 (1998).
Dobson, C.M. & Hore, P.J. Nature Struct. Biol. 5, 504–507 (1998).
Song, J. et al. Biochemistry 36, 3760–3766 (1997).
Drakopoulou, E. et al. Biochemistry 37, 1292– 1301 (1998).
Bontems, F., Roumestand, C., Gilquin, B., Menez, A. & Toma, F. Science 245, 1521–1523 (1991).
Bruix, M. et al. Biochemistry 32, 715– 724 (1993).
Caldwell, J. E. Nature Struct. Biol. 5, 427–431 (1998).
Menez, A., Bontems, F., Roumestand, C., Gilquin, B. & Toma, F. Proc. R. Soc. Edinburgh 99 B, 83–103 (1992 ).
Vita, C. Curr. Opin. Biotechnol. 8, 429–434 (1997).
Vita, C. et al. Biopolymers 47, 93–10 (1998).
Barrick, D., Hughson, F.M. & Baldwin, R.L. J. Mol. Biol. 237, 588– 601 (1994).
Redfield, C., Smith, R.A.G. & Dobson, C.M. Nature Struct. Biol. 1, 23– 29 (1994).
Ferrer, M., Barany, G. & Woodward, C. Nature Struct. Biol. 2, 211– 217 (1995).
Wishart, D.S., Sykes, B.D. & Richards, F.M. J. Mol. Biol. 222, 311– 333 (1991).
Ptitsyn, O. B. Adv. Protein Chem. 47, 83–229 (1995).
Eliezer, D., Jennings, P.A., Dyson, H.J. & Wright, P.E. FEBS Lett. 417, 92–96 ( 1997).
Gutin, A.M., Abkevich, V.I. & Shakhnovich, E.I. Biochemistry 34, 3066– 3076 (1995).
Oliveberg, M., Tan. Y.J., Silow, M. & Fersht,, A.R. J. Mol. Biol. 277, 933–943 ( 1998).
Kim, P.S. & Baldwin, R.L. Annu. Rev. Biochem. 51, 459–489 (1982).
Matthews, C.R. Annu. Rev. Biochem. 62 653–683 (1993).
Fersht, A.R. Curr. Opin. Struct. Biol. 7, 3–9 (1997).
Song, J., Bai, P., Luo, L. & Peng, Z. J. Mol. Biol. 280, 167–174 (1998).
Baldwin, R.L. Folding & Design 1, R1–8 (1996).
Kiefhaber, T. Labhardt, A.M. & Baldwin, R.L. Nature 375, 513– 515 (1995).
Hoeltzli, S.D. & Freiden, C. Proc. Natl. Acad. Sci. USA 92, 9318–9322 ( 1995).
Miller, C. Neuron, 15, 5–10 ( 1995).
Dauplais, M. et al. J. Biol. Chem. 272, 4302– 4309 (1997).
Zinn–Justin, S. et al. Biochemistry 35, 8535– 8543 (1996).
Plaxco, K.W. & Gross, M. Nature 386, 657–659 (1997).
David, D.G. & Bax, A. J. Am. Chem. Soc. 107, 2820–2821 (1985).
Kumar, A., Ernest, R.R. & Wüthrich, K. Biochem, Biophys. Res. Commun. 95, 1–6 (1980).
Plateau, P. & Gueron, M. J. Am. Chem. Soc. 104 , 7310 (1982).
Acknowledgements
We thank Z.Y. Peng, Department of Biochemistry, University of Connecticut Health Centre, for helpful discussion, and T. Sprules at the Biotechnology Research Institute for reading the manuscript.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Song, J., Jamin, N., Gilquin, B. et al. A gradual disruption of tight side–chain packing: 2D 1H–NMR characterization of acid–induced unfolding of CHABII . Nat Struct Mol Biol 6, 129–134 (1999). https://doi.org/10.1038/5815
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/5815
This article is cited by
-
ATP induces folding of ALS-causing C71G-hPFN1 and nascent hSOD1
Communications Chemistry (2023)
-
Environment-transformable sequence–structure relationship: a general mechanism for proteotoxicity
Biophysical Reviews (2018)