The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
A statistical mechanical model for β-hairpin kinetics
Open accessAbstract
Understanding the mechanism of protein secondary structure formation is an essential part of the protein-folding puzzle. Here, we describe a simple statistical mechanical model for the formation of a β-hairpin, the minimal structural element of the antiparallel β-pleated sheet. The model accurately describes the thermodynamic and kinetic behavior of a 16-residue, β-hairpin-forming peptide, successfully explaining its two-state behavior and apparent negative activation energy for folding. The model classifies structures according to their backbone conformation, defined by 15 pairs of dihedral angles, and is further simplified by considering only the 120 structures with contiguous stretches of native pairs of backbone dihedral angles. This single sequence approximation is tested by comparison with a more complete model that includes the 2 15 possible conformations and 15 × 2 15 possible kinetic transitions. Finally, we use the model to predict the equilibrium unfolding curves and kinetics for several variants of the β-hairpin peptide.
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Cites
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
Funnels, pathways, and the energy landscape of protein folding: A synthesis
Bryngelson, J. D., Onuchic, J. N., Socci, N. D., & Wolynes, P. G. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340210302 · Cited by 2,648
Cited by
Fast Kinetics and Mechanisms in Protein Folding
Eaton, W. A., Muñoz, V., Hagen, S. J., Jas, G. S., Lapidus, L. J., Henry, E. R., & Hofrichter, J. (2000) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.29.1.327 · Cited by 488
Self-citationMinimal model systems for β-sheet secondary structure in proteins
Gellman, S. H. (1998) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(98)80109-9 · Cited by 332
Understanding β-hairpin formation
Dinner, A. R., Lazaridis, T., & Karplus, M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.16.9068 · Cited by 326
The folding mechanism of a β-sheet: the WW domain
Jäger, M., Nguyen, H., Crane, J. C., Kelly, J. W., & Gruebele, M. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4873 · Cited by 302
Free energy landscape of protein folding in water: Explicit vs. implicit solvent
Zhou, R. (2003) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.10483 · Cited by 300
Metadata
- Authors
- Muñoz, V., Henry, E. R., Hofrichter, J., & Eaton, W. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1998-05-26
- Volume
- 95
- Issue
- 11
- Pages
- 5872-5879
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1966712500
- Cited by
- 334
- References
- 2
- FWCI
- 5.06
- Type
- journal article
- Language
- en
- Open access
- green
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- Muñoz, V., Henry, E. R., Hofrichter, J., & Eaton, W. A. (1998). A statistical mechanical model for β-hairpin kinetics. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.95.11.5872
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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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