The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Localizing frustration in native proteins and protein assemblies
Open accessAbstract
We propose a method of quantifying the degree of frustration manifested by spatially local interactions in protein biomolecules. This method of localization smoothly generalizes the global criterion for an energy landscape to be funneled to the native state, which is in keeping with the principle of minimal frustration. A survey of the structural database shows that natural proteins are multiply connected by a web of local interactions that are individually minimally frustrated. In contrast, highly frustrated interactions are found clustered on the surface, often near binding sites. These binding sites become less frustrated upon complex formation.
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Cites
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The Energy Landscapes and Motions of Proteins
Frauenfelder, H., Sligar, S. G., & Wolynes, P. G. (1991) · Science · doi:10.1126/science.1749933 · Cited by 3,250
Self-citationFunnels, 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
Self-citationStructure and Mechanism in Protein Science
Fersht, A. (1998) · Cited by 1,882
Spin glasses and the statistical mechanics of protein folding.
Bryngelson, J. D., & Wolynes, P. G. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.21.7524 · Cited by 1,634
Self-citationClementi, C., Nymeyer, H., & Onuchic, J. N. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3693 · Cited by 1,240
Oppenheimer, N. J., & James, T. L. (1989) · Academic Press eBooks · Cited by 820
Intermediates and barrier crossing in a random energy model (with applications to protein folding)
Bryngelson, J. D., & Wolynes, P. G. (1989) · The Journal of Physical Chemistry · doi:10.1021/j100356a007 · Cited by 755
Self-citationAnalysis of protein-protein interaction sites using surface patches 1 1Edited by G.Von Heijne
Jones, S., & Thornton, J. M. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1234 · Cited by 602
Toward an outline of the topography of a realistic protein-folding funnel.
Onuchic, J. N., Wolynes, P. G., Luthey-Schulten, Z., & Socci, N. D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.8.3626 · Cited by 523
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Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436
Coarse-grained models of protein folding: toy models or predictive tools?
Clementi, C. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.10.005 · Cited by 340
Ferreiro, D. U., Komives, E. A., & Wolynes, P. G. (2014) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583514000092 · Cited by 314
Self-citationPorebski, B. T., & Buckle, A. M. (2016) · Protein Engineering Design and Selection · doi:10.1093/protein/gzw015 · Cited by 215
Li, W., Wolynes, P. G., & Takada, S. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1018983108 · Cited by 159
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Metadata
- Authors
- Ferreiro, D. U., Hegler, J. A., Komives, E. A., & Wolynes, P. G.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2007-12-11
- Volume
- 104
- Issue
- 50
- Pages
- 19819-19824
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1991194470
- Cited by
- 360
- References
- 33
- FWCI
- 5.15
- Type
- journal article
- Language
- en
- Open access
- green
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- Ferreiro, D. U., Hegler, J. A., Komives, E. A., & Wolynes, P. G. (2007). Localizing frustration in native proteins and protein assemblies. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0709915104
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
