The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Evolution, energy landscapes and the paradoxes of protein folding
Open accessAbstract
Protein folding has been viewed as a difficult problem of molecular self-organization. The search problem involved in folding however has been simplified through the evolution of folding energy landscapes that are funneled. The funnel hypothesis can be quantified using energy landscape theory based on the minimal frustration principle. Strong quantitative predictions that follow from energy landscape theory have been widely confirmed both through laboratory folding experiments and from detailed simulations. Energy landscape ideas also have allowed successful protein structure prediction algorithms to be developed. The selection constraint of having funneled folding landscapes has left its imprint on the sequences of existing protein structural families. Quantitative analysis of co-evolution patterns allows us to infer the statistical characteristics of the folding landscape. These turn out to be consistent with what has been obtained from laboratory physicochemical folding experiments signalling a beautiful confluence of genomics and chemical physics.
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Cites
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
Self-citationThe relation between the divergence of sequence and structure in proteins.
Chothia, C., & Lesk, A. M. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04288.x · Cited by 2,458
Gilbert, W. (1978) · Nature · doi:10.1038/271501a0 · Cited by 2,300
From Levinthal to pathways to funnels
Dill, K. A., & Chan, H. S. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb0197-10 · Cited by 2,293
THEORY OF PROTEIN FOLDING: The Energy Landscape Perspective
Onuchic, J. N., Luthey-Schulten, Z., & Wolynes, P. G. (1997) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.48.1.545 · Cited by 2,210
Self-citationMorcos, F., Pagnani, A., Lunt, B., Bertolino, A., Marks, D. S., Sander, C., Zecchina, R., Onuchic, J. N., Hwa, T., & Weigt, M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111471108 · Cited by 1,434
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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
Self-citationFolding funnels and energy landscapes of larger proteins within the capillarity approximation
Wolynes, P. G. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.12.6170 · Cited by 218
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Cited by
The Hsp70–Hsp90 Chaperone Cascade in Protein Folding
Morán Luengo, T., Mayer, M. P., & Rüdiger, S. G. D. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.10.004 · Cited by 282
Root of the Tree: The Significance, Evolution, and Origins of the Ribosome
Bowman, J. C., Petrov, A. S., Frenkel-Pinter, M., Penev, P. I., & Williams, L. D. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00742 · Cited by 197
AF3Score: A Score-Only Adaptation of AlphaFold3 for Biomolecular Structure Evaluation
Liu, Y., Yu, Q., Wang, D., & Chen, M. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c00653 · Cited by 9
Metadata
- Authors
- Wolynes, P. G.
- Venue
- Biochimie
- Publisher
- Elsevier BV
- Published
- 2015-12
- Volume
- 119
- Pages
- 218-230
- ISSN
- 0037-9042 (ISSN-L)
- 0300-9084
- OpenAlex
- W2087786915
- Cited by
- 180
- References
- 9
- FWCI
- 6.33
- Type
- journal article
- Language
- en
- Open access
- bronze
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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.
