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The Protein Folding Problem
Open accessAbstract
The "protein folding problem" consists of three closely related puzzles: (a) What is the folding code? (b) What is the folding mechanism? (c) Can we predict the native structure of a protein from its amino acid sequence? Once regarded as a grand challenge, protein folding has seen great progress in recent years. Now, foldable proteins and nonbiological polymers are being designed routinely and moving toward successful applications. The structures of small proteins are now often well predicted by computer methods. And, there is now a testable explanation for how a protein can fold so quickly: A protein solves its large global optimization problem as a series of smaller local optimization problems, growing and assembling the native structure from peptide fragments, local structures first.
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“The statistical energy landscape theory was developed to study protein folding.1,128–131”
From Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell (2016) · cites this paper as [130]
In the citing paper
“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 [51]
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“Levinthal argued that there is no need to search this vast space since the energy landscape is funnel-like, rather than flat, and thus can guide sampling toward the biological conformational basin.”
From AlphaFold, Artificial Intelligence (AI), and Allostery (2022) · cites this paper as [51]
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Citations
Cites
A Second Generation Force Field for the Simulation of Proteins, Nucleic Acids, and Organic Molecules
Cornell, W. D., Cieplak, P., Bayly, C. I., Gould, I. R., Merz, K. M., Ferguson, D. M., Spellmeyer, D. C., Fox, T., Caldwell, J. W., & Kollman, P. A. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00124a002 · Cited by 13,111
Comparative Protein Modelling by Satisfaction of Spatial Restraints
Šali, A., & Blundell, T. L. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1626 · Cited by 12,977
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
THE weighted histogram analysis method for free‐energy calculations on biomolecules. I. The method
Kumar, S., Rosenberg, J. M., Bouzida, D., Swendsen, R. H., & Kollman, P. A. (1992) · Journal of Computational Chemistry · doi:10.1002/jcc.540130812 · Cited by 6,808
Replica-exchange molecular dynamics method for protein folding
Sugita, Y., & Okamoto, Y. (1999) · Chemical Physics Letters · doi:10.1016/s0009-2614(99)01123-9 · Cited by 4,499
Dominant forces in protein folding
Dill, K. A. (1990) · Biochemistry · doi:10.1021/bi00483a001 · Cited by 3,829
Self-citationPrediction of protein conformation
Chou, P. Y., & Fasman, G. D. (1974) · Biochemistry · doi:10.1021/bi00699a002 · Cited by 3,309
Empirical Predictions of Protein Conformation
Chou, P. Y., & Fasman, G. D. (1978) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.47.070178.001343 · Cited by 3,137
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
Gellman, S. H. (1998) · Accounts of Chemical Research · doi:10.1021/ar960298r · Cited by 2,550
Research works printed but not linked: 2
- Grabowski M, 2007, Nucleic Acids Seq. Topol., 17, 347
- Hubner IA, 2003, Abstr. Pap. Am. Chem. Soc., 226, U450
Cited by
Sorted by citations
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Balasco, N., Smaldone, G., Vigorita, M., Vecchio, P. D., Graziano, G., Ruggiero, A., & Vitagliano, L. (2019) · Scientific Reports · doi:10.1038/s41598-019-43157-y · Cited by 9
Lonsdale, D. (2019) · Medical Hypotheses · doi:10.1016/j.mehy.2019.109252 · Cited by 9
Using contact statistics to characterize structure transformation of biopolymer ensembles
Das, P., Golloshi, R., McCord, R. P., & Shen, T. (2020) · Physical review. E · doi:10.1103/physreve.101.012419 · Cited by 9
Culka, M., & Rulı́šek, L. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.9b11784 · Cited by 9
Bel-Hadj-Aissa, G., Gori, M., Franzosi, R., & Pettini, M. (2021) · Journal of Statistical Mechanics Theory and Experiment · doi:10.1088/1742-5468/abda27 · Cited by 9
Ma, X., Sun, H., Hong, H., Guo, Z., Su, H., & Chen, H. (2022) · Physical review. E · doi:10.1103/physreve.106.024404 · Cited by 10
Roles of Intramolecular Interactions in the Regulation of TRP Channels
Cai, R., & Chen, X. (2022) · Reviews of physiology, biochemistry and pharmacology · doi:10.1007/112_2022_74 · Cited by 9
Shin, J. H., Bonilla, S. L., Denny, S. K., Greenleaf, W. J., & Herschlag, D. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2220485120 · Cited by 8
Artificial intelligence in precision medicine
Siddiqui, S. S., Loganathan, S., Elangovan, V. R., & Ali, M. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-89925-3.00020-4 · Cited by 10
Pan, H., Raab, S. A., El‐Baba, T. J., Schrecke, S. R., Laganowsky, A. D., Russell, D. H., & Clemmer, D. E. (2023) · The Journal of Physical Chemistry A · doi:10.1021/acs.jpca.3c03651 · Cited by 9
Qiu, S., Li, G., Wang, P., Jia, G., Feng, Z., & Li, C. (2011) · Journal of Raman Spectroscopy · doi:10.1002/jrs.3056 · Cited by 9
Simulating Biomolecular Folding and Function by Native‐Structure‐Based/Go‐Type Models
Sinner, C., Lutz, B., John, S., Reinartz, I., Verma, A., & Schug, A. H. (2014) · Israel Journal of Chemistry · doi:10.1002/ijch.201400012 · Cited by 10
The Roles of Entropy and Kinetics in Structure Prediction
Bowman, G. R., & Pande, V. S. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005840 · Cited by 9
Computer Simulations of Protein Folding
Javidpour, L. (2012) · Computing in Science & Engineering · doi:10.1109/mcse.2012.21 · Cited by 9
Fabrication of Chiral Materials via Self‐Assembly and Biomineralization of Peptides
Huang, Z., & Che, S. (2015) · The Chemical Record · doi:10.1002/tcr.201402096 · Cited by 9
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Stockmar, F., Kobitski, A. Y., & Nienhaus, G. U. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b09336 · Cited by 9
Drobnak, I., Ljubetič, A., Gradišar, H., Pisanski, T., & Jerala, R. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-39196-0_2 · Cited by 9
Joseph, J. A., Whittleston, C. S., & Wales, D. J. (2016) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.6b00734 · Cited by 9
Soranno, A., Cabassi, F., Orselli, M. E., Cellmer, T., Gori, A., Longhi, R., & Buscaglia, M. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b07399 · Cited by 9
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Flanagan, J. C., & Baiz, C. R. (2019) · Optics Letters · doi:10.1364/ol.44.004937 · Cited by 9
Efficient Coarse-Grained Molecular Simulations in the Multibody Dynamics Scheme
Poursina, M., & Anderson, K. S. (2012) · Computational methods in applied sciences · doi:10.1007/978-94-007-5404-1_7 · Cited by 9
DeepSF: deep convolutional neural network for mapping protein sequences to foldsPreprint
Hou, J., Adhikari, B., & Cheng, J. J. (2017) · arXiv (Cornell University) · doi:10.48550/arxiv.1706.01010 · Cited by 9
Building Markov state models using optimal transport theory
Dixit, P. D., & Dill, K. A. (2019) · The Journal of Chemical Physics · doi:10.1063/1.5086681 · Cited by 9
Self-citationRoterman, I., Stąpor, K., Dułak, D., & Konieczny, L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23169502 · Cited by 8
Beyond Misfolding: A New Paradigm for the Relationship Between Protein Folding and Aggregation
Choi, S. I., Jin, Y., Choi, Y., & Seong, B. L. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms26010053 · Cited by 9
Li, G., Zhou, J., Luo, J., & Liang, C. (2025) · BMC Genomics · doi:10.1186/s12864-025-11694-8 · Cited by 9
Protein Misfolding and Aggregation of Tau Protein in Alzheimer’s Disease
Chandrashekar, M., & Chinnathambi, S. (2020) · Springer eBooks · doi:10.1007/978-981-15-2063-1_8 · Cited by 8
Smoothing Protein Energy Landscapes by Integrating Folding Models with Structure Prediction
Pritchard‐Bell, A., & Shell, M. S. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.09.036 · Cited by 8
Self-citationKhan, I. M., Poursina, M., & Anderson, K. S. (2013) · Computer Physics Communications · doi:10.1016/j.cpc.2013.02.025 · Cited by 8
Design and Fabrication of DNA Origami Mechanisms and Machines
Su, H., Castro, C. E., Marras, A. E., & Hudoba, M. W. (2012) · Springer eBooks · doi:10.1007/978-1-4471-4141-9_44 · Cited by 8
Markiewicz, B. N., Culik, R. M., & Gai, F. (2014) · Science China Chemistry · doi:10.1007/s11426-014-5225-5 · Cited by 8
Dai, J., Niemi, A. J., & He, J. (2016) · The Journal of Chemical Physics · doi:10.1063/1.4959582 · Cited by 8
Chakraborty, H. J., Gangopadhyay, A., Ganguli, S., & Datta, A. (2017) · Advances in bioinformatics and biomedical engineering book series · doi:10.4018/978-1-5225-2607-0.ch003 · Cited by 8
Fischer, J. L., Elvir, B. R., DeLucia, S.-A., Blodgett, K. N., Zeller, M., Kubasik, M. A., & Zwier, T. S. (2019) · The Journal of Physical Chemistry A · doi:10.1021/acs.jpca.9b01698 · Cited by 8
Small Neutral Crowding Solute Effects on Protein Folding Thermodynamic Stability and Kinetics
Contessoto, V. G., Ferreira, P. H. B., Chahine, J., Leite, V. B. P., & de Oliveira, R. J. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c07663 · Cited by 8
The Complexity of Protein Structure and the Challenges it Poses in Developing Biopharmaceuticals
Berkowitz, S. A., & Houde, D. J. (2014) · Elsevier eBooks · doi:10.1016/b978-0-444-59573-7.00001-4 · Cited by 8
Reduced atomic pair-interaction design (RAPID) model for simulations of proteins
Ni, B., & Baumketner, A. (2013) · The Journal of Chemical Physics · doi:10.1063/1.4790160 · Cited by 8
Protein folding: interplay of hydrophobic–hydrophilic forces?
Joshi, R. (2013) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2012.748530 · Cited by 8
Rocha, J. R., van der Linden, M. G., Ferreira, D. C., Azevêdo, P. H., & de Araújo, A. F. P. (2012) · Bioinformatics · doi:10.1093/bioinformatics/bts512 · Cited by 8
A novel topology for representing protein folds
Segal, M. R. (2009) · Protein Science · doi:10.1002/pro.90 · Cited by 8
A highly efficient hybrid method for calculating the hydration free energy of a protein
Oshima, H., & Kinoshita, M. (2015) · Journal of Computational Chemistry · doi:10.1002/jcc.24253 · Cited by 8
Merstorf, C., Maciejak, O., Mathé, J., Pastoriza‐Gallego, M., Thiébot, B., Clément, M., Pelta, J., Auvray, L., Curmi, P. A., & Savarin, P. (2012) · Biochemistry · doi:10.1021/bi3003605 · Cited by 8
Shao, Q., & Zhu, W. (2017) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.7b00242 · Cited by 8
Side chain flexibility and the symmetry of protein homodimers
Shalit, Y., & Tuvi‐Arad, I. (2020) · PLoS ONE · doi:10.1371/journal.pone.0235863 · Cited by 8
Industrial Enzymes and Biocatalysis
McAuliffe, J. C. (2012) · Springer eBooks · doi:10.1007/978-1-4614-4259-2_31 · Cited by 8
Mapping Protein Structural Evolution upon Unfolding
Avadhani, V. S., Mondal, S., & Banerjee, S. (2022) · Biochemistry · doi:10.1021/acs.biochem.1c00743 · Cited by 8
Standardized evaluation of protein stability
Thomas, A., Joris, B., & Brasseur, R. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.02.008 · Cited by 8
Balasco, N., Esposito, L., & Vitagliano, L. (2025) · Biomolecules · doi:10.3390/biom15050674 · Cited by 6
Dramatic Shape Changes Occur as Cytochrome c Folds
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Balasco, N., Esposito, L., Simone, A. D., & Vitagliano, L. (2022) · Biomolecules · doi:10.3390/biom12091184 · Cited by 7
Pradhan, R., Panigrahi, S., & Sahu, P. K. (2023) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.2c01398 · Cited by 7
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Priyadarshi, A., Devi, H. M., & Swaminathan, R. (2023) · Biochemistry · doi:10.1021/acs.biochem.3c00006 · Cited by 7
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Loparo, J. J., & van Oijen, A. M. (2009) · Springer eBooks · doi:10.1007/978-0-387-76497-9_6 · Cited by 7
Pink, D. A., & Razul, M. S. G. (2013) · Food Structure · doi:10.1016/j.foostr.2013.11.005 · Cited by 7
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Yang, X., Liu, J., Xie, Y. L., Wang, Y., Ying, H., Wu, Q., Huang, W., & Jenkins, G. N. (2014) · The Analyst · doi:10.1039/c4an00173g · Cited by 7
Chekmarev, S. F. (2015) · PLoS ONE · doi:10.1371/journal.pone.0121640 · Cited by 7
Banerjee, A., Pal, K., & Mitra, P. (2019) · IEEE Transactions on Computational Biology and Bioinformatics · doi:10.1109/tcbb.2019.2928809 · Cited by 7
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Horn, T. L., Ivanov, I., Venere, A. D., Kakularam, K. R., Reddanna, P., Conrad, M. L., Richter, C., Scheerer, P., & Kühn, H. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.08.004 · Cited by 6
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Micro-viscosity induced conformational transitions in poly- l -lysine
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Olivares‐Quiroz, L. (2013) · Journal of Physics Condensed Matter · doi:10.1088/0953-8984/25/15/155103 · Cited by 6
Faccioli, R. A., da Silva, I. N., Bortot, L. O., & Delbem, A. C. B. (2012) · IEEE Congress on Evolutionary Computation (CEC) · doi:10.1109/cec.2012.6256625 · Cited by 6
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Solvent-induced forces in protein folding reflections on the protein folding problem
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Fields, F. R., Suresh, N., Hiller, M., Freed, S. D., Haldar, K., & Lee, S. W. (2020) · PLoS ONE · doi:10.1371/journal.pone.0234100 · Cited by 6
The structural biology of crystallin aggregation: challenges and outlook
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McDonald, J., von Spakovsky, M. R., & Reynolds, W. T. (2023) · The Journal of Chemical Physics · doi:10.1063/5.0137444 · Cited by 6
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Refolding of SDS‐Denatured Proteins Using Amphipathic Cosolvents and Osmolytes
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Pérez, J. J. (2011) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/073911011010524980 · Cited by 6
Understanding the Mechanism of Prosegment-catalyzed Folding by Solution NMR Spectroscopy
Wang, S., Horimoto, Y., Dee, D. R., & Yada, R. Y. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.505891 · Cited by 6
Characterization of the unfolded state of repeat proteins
Mor, A., Haran, G., & Levy, Y. (2008) · HFSP journal · doi:10.2976/1.3021145 · Cited by 6
Glembo, T. J., & Ozkan, S. B. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2009.11.031 · Cited by 6
Self-citationWu, T., Yang, L., Zhang, R., Shao, Q., & Zhuang, W. (2013) · The Journal of Physical Chemistry A · doi:10.1021/jp400625a · Cited by 6
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Metadata
- Authors
- Dill, K. A., Ozkan, S. B., Shell, M. S., & Weikl, T. R.
- Affiliations
- University of California, San Francisco (US)
- Arizona State University (US)
- University of California, Santa Barbara (US)
- Max Planck Institute of Colloids and Interfaces (DE)
- Venue
- Annual Review of Biophysics
- Publisher
- Annual Reviews
- Published
- 2008-06-01
- Volume
- 37
- Issue
- 1
- Pages
- 289-316
- ISSN
- 1936-122X (ISSN-L)
- 1936-1238
- PMC
- PMC2443096
- OpenAlex
- W2129020329
- Cited by
- 1,163
- References
- 248
- Citations by year
- 2026: 51 · 2025: 61 · 2024: 60 · 2023: 70 · 2022: 73 · 2021: 73 · 2020: 59 · 2019: 53 · 2018: 52 · 2017: 47 · 2016: 48 · 2015: 43 · 2014: 70 · 2013: 82 · 2012: 78
- FWCI
- 6.04
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Annual Review of Biophysics (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Max Planck Digital Library (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- 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 mechanism, protein structure prediction, de novo protein design, peptide fragments, local optimization, global optimization, folding rate
- MeSH terms
- Computer Simulation, Models, Chemical, Models, Molecular, Protein Conformation, Proteins, Protein Folding
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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