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NMR Determination of Residual Structure in a Urea-Denatured Protein, the 434-Repressor
Abstract
A nuclear magnetic resonance (NMR) structure determination is reported for the polypeptide chain of a globular protein in strongly denaturing solution. Nuclear Overhauser effect (NOE) measurements with a 7 molar urea solution of the amino-terminal 63-residue domain of the 434-repressor and distance geometry calculations showed that the polypeptide segment 54 to 59 forms a hydrophobic cluster containing the side chains of Val 54 , Val 56 , Trp 58 , and Leu 59 . This residual structure in the urea-unfolded protein is related to the corresponding region of the native, folded protein by simple rearrangements of the residues 58 to 60. Based on these observations a model for the early phase of refolding of the 434-repressor(1-63) is proposed.
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Cited by
Valence and patterning of aromatic residues determine the phase behavior of prion-like domains
Martin, E. W., Holehouse, A. S., Peran, I., Farag, M., Incicco, J. J., Bremer, A., Grace, C. R., Soranno, A., Pappu, R. V., & Mittag, T. (2020) · Science · doi:10.1126/science.aaw8653 · Cited by 1,147
Bernadó, P., Blanchard, L., Timmins, P., Marion, D., Ruigrok, R. W. H., & Blackledge, M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506202102 · Cited by 441
Reversible peptide folding in solution by molecular dynamics simulation 1 1Edited by R. Huber
Daura, X., Jaun, B., Seebach, D., van Gunsteren, W. F., & Mark, A. E. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1885 · Cited by 373
De novo design of the hydrophobic cores of proteins
Desjarlais, J. R., & Handel, T. M. (1995) · Protein Science · doi:10.1002/pro.5560041006 · Cited by 306
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Fisher, C. K., & Stultz, C. M. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.04.001 · Cited by 275
Metadata
- Authors
- Neri, D., Billeter, M., Wider, G., & Wüthrich, K.
- Venue
- Science
- Published
- 1992-09-11
- Volume
- 257
- Issue
- 5076
- Pages
- 1559-1563
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1996222219
- Cited by
- 448
- References
- 0
- FWCI
- 8.78
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: NMR Determination of Residual Structure in a Urea-Denatured Protein, the 434-Repressor. https://app.cochat.ai/papers/10.1126/science.1523410
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- Neri, D., Billeter, M., Wider, G., & Wüthrich, K. (1992). NMR Determination of Residual Structure in a Urea-Denatured Protein, the 434-Repressor. Science. https://doi.org/10.1126/science.1523410
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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