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The Protein-Folding Problem, 50 Years On
Abstract
Protein Folding: Past and Future: Fifty years ago the Nobel Prize in chemistry was awarded to Max Perutz and John Kendrew for determining the structure of globular proteins. Since first viewing their structure of myoglobin, scientists have sought to understand protein folding. Dill and MacCallum (p. 1042 ) review the progress that has been made on three central questions: What is the code that relates sequence to structure? How do proteins fold so fast? Can protein structure be computationally predicted? While we have come some way toward answering these questions, new questions have been gene rated. It is no longer useful to talk about “solving the protein-folding problem”—protein folding has grown into a field of research where the next 50 years promise to be as exciting as the last.
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“AlphaFold does not resolve the decades-long protein folding challenge, nor does it identify the folding pathways.”
From AlphaFold, Artificial Intelligence (AI), and Allostery (2022) · cites this paper as [52]
In the citing paper
“According to the funnel hypothesis of protein folding, the native structure of a protein is believed to the global minimum of its free energy [177,193], although many counterexamples exist.”
From The prospects of quantum computing in computational molecular biology (2021) · cites this paper as [177]
In the citing paper
“In fact, as has often been pointed out (for example43) this is a fallacious argument, since the free energy falls progressively as the protein folds, providing sufficient guidance44.”
From Critical assessment of methods of protein structure prediction (CASP)—Round XIV (2021) · cites this paper as [44]
Citations
Cites
Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
Altschul, S. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.17.3389 · Cited by 73,302
Berman, H. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.235 · Cited by 40,196
Murzin, A. G., Brenner, S. E., Hubbard, T., & Chothia, C. (1995) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80134-2 · Cited by 6,435
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
Dominant forces in protein folding
Dill, K. A. (1990) · Biochemistry · doi:10.1021/bi00483a001 · Cited by 3,829
Self-citationThe HHpred interactive server for protein homology detection and structure prediction
Söding, J., Biegert, A., & Lupas, A. N. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki408 · Cited by 3,775
The structure of proteins: Two hydrogen-bonded helical configurations of the polypeptide chain
Pauling, L. C., Corey, R. B., & Branson, H. R. (1951) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.37.4.205 · Cited by 3,007
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
Gellman, S. H. (1998) · Accounts of Chemical Research · doi:10.1021/ar960298r · Cited by 2,550
Flagged first, then by citations
Research works printed but not linked: 2
- Englander S. W., Mayne L., Krishna M. M. G., Q. Rev. Biophys. 40, 287 (2008).
- Snow C. D., Nguyen H., Pande V. S., Gruebele M., Nat. Struct. Mol. Biol. 420, 102 (2002).
Cited by
Sorted by citations
Items 501–600 of 1,001
Oikawa, H., Kamagata, K., Arai, M., & Takahashi, S. (2015) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b00414 · Cited by 19
GdnHCl-induced unfolding intermediate in the mitochondrial carbonic anhydrase VA
Idrees, D., Prakash, A., Haque, M. A., Islam, A., Hassan, M. I., & Ahmad, F. (2016) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2016.06.080 · Cited by 19
Hsu, D. J., Leshchev, D., Rimmerman, D., Hong, J., Kelley, M. S., Kosheleva, I. V., Zhang, X., & Chen, L. X. (2019) · Chemical Science · doi:10.1039/c9sc02630d · Cited by 19
Sever, A. I. M., & Konermann, L. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c01934 · Cited by 19
Entropy-Enthalpy Compensations Fold Proteins in Precise Ways
Li, J., Hou, C., Ma, X., Guo, S., Zhang, H., Shi, L., Liao, C., Zheng, B., Ye, L., Yang, L., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179653 · Cited by 19
Forecasting emergence of COVID-19 variants of concern
Miller, J. K., Elenberg, K., & Dubrawski, A. W. (2022) · PLoS ONE · doi:10.1371/journal.pone.0264198 · Cited by 19
Gradual Folding of an Off-Pathway Molten Globule Detected at the Single-Molecule Level
Lindhoud, S., Pirchi, M., Westphal, A. H., Haran, G., & van Mierlo, C. P. M. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.07.002 · Cited by 19
Backbone Hydration Determines the Folding Signature of Amino Acid Residues
Bignucolo, O., Leung, H. T. A., Grzesiek, S., & Bernèche, S. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b00660 · Cited by 19
Construction of protein-functionalized virus-like particles of parvovirus B19
Bustos‐Jaimes, I., Soto-Román, R. A., Gutiérrez-Landa, I. A., Valadez-García, J., & Segovia-Trinidad, C. L. (2017) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2017.09.014 · Cited by 19
Galano‐Frutos, J. J., & Sancho, J. (2024) · Protein Science · doi:10.1002/pro.4905 · Cited by 19
Binding adaptability of chemical ligands to polymorphic α-synuclein amyloid fibrils
Liu, K., Tao, Y., Zhao, Q., Xia, W., Li, X., Zhang, S., Yao, Y., Xiang, H., Han, C., Tan, L., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2321633121 · Cited by 21
Large language models design sequence-defined macromolecules via evolutionary optimization
Reinhart, W. F., & Statt, A. (2024) · npj Computational Materials · doi:10.1038/s41524-024-01449-6 · Cited by 20
Niazi, S. (2025) · Computational and Structural Biotechnology Reports · doi:10.1016/j.csbr.2025.100064 · Cited by 20
Peierls-Nabarro barrier and protein loop propagation
Sieradzan, A. K., Niemi, A. J., & Peng, X. (2014) · Physical Review E · doi:10.1103/physreve.90.062717 · Cited by 18
VTR: A Web Tool for Identifying Analogous Contacts on Protein Structures and Their Complexes
Pimentel, V., Mariano, D., Cantão, L. X. S., Bastos, L. L., Fischer, P., de Lima, L. H. F., Fassio, A. V., & de Melo-Minardi, R. C. (2021) · Frontiers in Bioinformatics · doi:10.3389/fbinf.2021.730350 · Cited by 18
Rohmer, M., Freudenberg, J., & Binder, W. H. (2022) · Macromolecular Bioscience · doi:10.1002/mabi.202200344 · Cited by 18
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Kocher, C. D., & Dill, K. A. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2218390120 · Cited by 18
Self-citationOrigins of life: first came evolutionary dynamics
Kocher, C. D., & Dill, K. A. (2023) · QRB Discovery · doi:10.1017/qrd.2023.2 · Cited by 18
Self-citationStructure and Dynamics Guiding Design of Antibody Therapeutics and Vaccines
Fernández‐Quintero, M. L., Pomarici, N. D., Fischer, A.-L. M., Hoerschinger, V. J., Kroell, K. B., Riccabona, J. R., Kamenik, A. S., Loeffler, J. R., Ferguson, J. A., Perrett, H. R., et al. (2023) · Antibodies · doi:10.3390/antib12040067 · Cited by 21
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Hamuro, Y. (2024) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.4c00044 · Cited by 18
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Majumder, S., & Wolfhard Janke, E. (2016) · Physical review. E · doi:10.1103/physreve.93.032506 · Cited by 18
A growing toolbox of techniques for studying β-barrel outer membrane protein folding and biogenesis
Horne, J. E., & Radford, S. E. (2016) · Biochemical Society Transactions · doi:10.1042/bst20160020 · Cited by 17
Zhou, X., Zhang, G., Hao, X., Xu, D., & Yu, L. J. (2016) · Applied Soft Computing · doi:10.1016/j.asoc.2016.06.044 · Cited by 18
Matriarch: A Python Library for Materials Architecture
Giesa, T., Jagadeesan, R., Spivak, D. I., & Buehler, M. J. (2015) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.5b00251 · Cited by 17
Шайтан, К. В., Lozhnikov, M., & Kobelkov, G. M. (2016) · BIOPHYSICS · doi:10.1134/s0006350916040205 · Cited by 18
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Liu, Z., Reddy, G., & Thirumalai, D. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b00327 · Cited by 17
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Shi, Q., Zhang, Y., Huang, Z., Zhou, N., Zhang, Z., & Zhu, X. (2019) · Polymer Journal · doi:10.1038/s41428-019-0263-7 · Cited by 18
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Wang, J., Karki, C. B., Xiao, Y., & Li, L. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2020.01.014 · Cited by 18
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Tan, J., Ni, Z., & Ye, S. (2022) · The Journal of Chemical Physics · doi:10.1063/5.0078632 · Cited by 18
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Chen, J.-H., Chi, M., Lin, M.-G., Lin, L., & Wang, T. (2015) · BioMed Research International · doi:10.1155/2015/806847 · Cited by 18
Falk, B. G., Snow, R. W., & Reed, R. N. (2016) · Southeastern Naturalist · doi:10.1656/058.015.sp806 · Cited by 18
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Houwman, J. A., & van Mierlo, C. P. M. (2017) · FEBS Journal · doi:10.1111/febs.14077 · Cited by 20
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Neelamraju, S., Wales, D. J., & Gosavi, S. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.07.003 · Cited by 17
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Li, Q., Scholl, Z. N., & Marszałek, P. E. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201407211 · Cited by 17
Hassan, M., Abbas, Q., Raza, H., Moustafa, A. A., & Seo, S. (2017) · Molecular BioSystems · doi:10.1039/c7mb00211d · Cited by 17
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Taguchi, H., & Koike‐Takeshita, A. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1091677 · Cited by 18
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Hu, Y., Yang, H., Li, M., Zhong, Z., Zhou, Y., Bai, F., & Wang, Q. (2024) · Advanced Science · doi:10.1002/advs.202400884 · Cited by 17
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Mas, G., & Hiller, S. (2018) · FEMS Microbiology Letters · doi:10.1093/femsle/fny121 · Cited by 15
Wang, J., & Ferguson, A. L. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b08800 · Cited by 17
Freitas, F. C., Lima, A. N., Contessoto, V. G., Whitford, P. C., & de Oliveira, R. J. (2019) · The Journal of Chemical Physics · doi:10.1063/1.5113499 · Cited by 17
Combining molecular dynamics simulations and experimental analyses in protein misfolding
Wille, H., Dorosh, L., Amidian, S., Schmitt‐Ulms, G., & Stepanova, M. (2019) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2019.10.001 · Cited by 17
Qiu, J., Bai, X., Zhang, W., Ma, M., Wang, W., Ye, L., Wang, H., Tian, J., & Yu, P. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.853993 · Cited by 17
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Corrales, M., Cuscó, P., Usmanova, D. R., Chen, H., Bogatyreva, N. S., Filion, G. J. P., & Ivankov, D. N. (2015) · PLoS ONE · doi:10.1371/journal.pone.0143166 · Cited by 19
Chakraborty, S., Endres, K. J., Bera, R., Wojtas, Ł., Moorefield, C. N., Saunders, M. J., Das, N., Wesdemiotis, C., & Newkome, G. R. (2018) · Dalton Transactions · doi:10.1039/c7dt04571a · Cited by 17
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Hao, X., Zhang, G., Zhou, X., & Yu, X.-F. (2015) · IEEE Transactions on Computational Biology and Bioinformatics · doi:10.1109/tcbb.2015.2497226 · Cited by 16
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Chen, Y., Wang, Q., Zhang, C., Li, X., Gao, Q., Dong, C., Liu, Y., & Su, Z. G. (2016) · Protein Expression and Purification · doi:10.1016/j.pep.2016.01.015 · Cited by 16
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Guinn, E. J., & Marqusee, S. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.07.022 · Cited by 15
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Bhattacharya, S., & Bhattacharya, D. (2020) · Scientific Reports · doi:10.1038/s41598-020-59834-2 · Cited by 16
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Fang, C., Li, Z., Xu, D. H., & Shang, Y. (2019) · Bioinformatics · doi:10.1093/bioinformatics/btz712 · Cited by 15
Metadata
- Authors
- Dill, K. A., & MacCallum, J. L.
- Affiliations
- Stony Brook University (US)
- Corresponding author
- Dill, Ken A.
- Venue
- Science
- Published
- 2012-11-23
- Volume
- 338
- Issue
- 6110
- Pages
- 1042-1046
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2014050554
- Cited by
- 1,699
- References
- 72
- Citations by year
- 2026: 140 · 2025: 132 · 2024: 117 · 2023: 148 · 2022: 114 · 2021: 137 · 2020: 123 · 2019: 144 · 2018: 111 · 2017: 123 · 2016: 121 · 2015: 119 · 2014: 94 · 2013: 73 · 2012: 1
- FWCI
- 8.37
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM34993, R01GM034993)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- protein folding, folding kinetics, folding funnel, energy landscape, thermal fluctuations, protein structure prediction, Protein Data Bank
- MeSH terms
- Amino Acid Sequence, Computer Simulation, Pharmaceutical Preparations, Models, Chemical, Protein Conformation, Proteins, Protein Folding, Caspase 9
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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