THE KINETICS OF FORMATION OF NATIVE RIBONUCLEASE DURING OXIDATION OF THE REDUCED POLYPEPTIDE CHAIN
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Proceedings of the National Academy of Sciences (PNAS), a peer reviewed journal of the National Academy of Sciences (NAS) - an authoritative source of high-impact, original research that broadly spans the biological, physical, and social sciences.
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The folding paradigm stipulated that unfolded molecules spontaneously fold into the same shape, with the linear amino acid sequence specifying the folded native state.
“The folding paradigm stipulated that unfolded molecules will always spontaneously fold into the same shape; that is, the linear amino acid sequence specifies a protein’s folded native state.”
From AlphaFold, Artificial Intelligence (AI), and Allostery (2022) · cites this paper as [144]
Cites
Studies on the Reduction and Re-formation of Protein Disulfide Bonds
Anfinsen, C. B., & Haber, E. (1961) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64177-8 · Cited by 603 · see citing works
Self-citationA CHROMATOGRAPHIC INVESTIGATION OF PANCREATIC RIBONUCLEASE
Hirs, C. H. W., Moore, S., & Stein, W. H. (1953) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71393-8 · Cited by 534 · see citing works
THE PREPARATION AND CHARACTERIZATION OF RIBONUCLEIC ACIDS FROM YEAST
Crestfield, A. M., Smith, K. C., & Allen, F. W. (1955) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52295-5 · Cited by 440 · see citing works
STUDIES ON THE GROSS STRUCTURE, CROSS-LINKAGES, AND TERMINAL SEQUENCES IN RIBONUCLEASE
Anfinsen, C. B., Redfield, R. R., Choate, W. L., Page, J., & Carroll, W. R. (1954) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71260-x · Cited by 430 · see citing works
Self-citationSome spectrophotometric and polarimetric experiments with ribonuclease
Sela, M., & Anfinsen, C. B. (1957) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(57)90186-5 · Cited by 291 · see citing works
Self-citationRegeneration of Native Secondary and Tertiary Structures by Air Oxidation of Reduced Ribonuclease
Frederick, H., Bello, J., Harker, D., et al. (1961) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64176-6 · Cited by 284 · see citing works
The correlation of ribonuclease activity with specific aspects of tertiary structure
Sela, M., Anfinsen, C. B., & Harrington, W. F. (1957) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(57)90096-3 · Cited by 237 · see citing works
Self-citationThe reductive cleavage of disulfide bonds and its application to problems of protein structure
Sela, M., White, F. H., & Anfinsen, C. B. (1959) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(59)90016-2 · Cited by 170 · see citing works
Self-citationThe Isolation and Characterization of Ribonucleases from Sheep Pancreas
Åqvist, S. E. G., & Anfinsen, C. B. (1959) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98141-x · Cited by 86 · see citing works
Self-citationAn assay for ribonuclease activity using a cyclic phosphate substrate.
Fm, R. (1955) · PubMed · Cited by 6 · see citing works
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Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096 · see citing works
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 · see citing works
“Soon after Anfinsen’s classic experiments on renaturation of unfolded proteins [1], Levinthal recognized the conceptual difficulty of a molecule searching at random through the cosmologically large number of unfolded configurations to find the folded structure in a biologically relevant time [2].”
BackgroundFrom 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 · see citing works
Consistent blind protein structure generation from NMR chemical shift data
Shen, Y., Lange, O., Delaglio, F., Rossi, P., Aramini, J. M., Liu, G., Eletsky, A., Wu, Y., Singarapu, K. K., Lemak, A., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800256105 · Cited by 855 · see citing works
Advances in protein structure prediction and design
Kuhlman, B., & Bradley, P. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0163-x · Cited by 806 · see citing works
Evaluating Protein Transfer Learning with TAPE
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Shea, J.-E., & Brooks III, C. L. (2001) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.52.1.499 · Cited by 481 · see citing works
Single-sequence protein structure prediction using a language model and deep learning
Chowdhury, R., Bouatta, N., Biswas, S., Floristean, C., Kharkar, A., Roy, K., Rochereau, C., Ahdritz, G., Zhang, J., Church, G. M., et al. (2022) · Nature Biotechnology · doi:10.1038/s41587-022-01432-w · Cited by 455 · see citing works
Single-sequence protein structure prediction using language models from deep learning
Chowdhury, R., Bouatta, N., Biswas, S., Rochereau, C., Church, G. M., Sorger, P. K., & AlQuraishi, M. (2021) · doi:10.1101/2021.08.02.454840 · Cited by 455 · see citing works
“It has been known since Anfinsen’s refolding experiments that single polypeptide chains contain the information needed to specify fold 46 .”
BackgroundBowman, G. R., Beauchamp, K. A., Boxer, G., & Pande, V. S. (2009) · The Journal of Chemical Physics · doi:10.1063/1.3216567 · Cited by 396 · see citing works
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Roney, J. P., & Ovchinnikov, S. (2022) · Physical Review Letters · doi:10.1103/physrevlett.129.238101 · Cited by 281 · see citing works
Side-chain Interactions Governing the Pairing of Half-cystine Residues in Ribonuclease
Haber, E., & Anfinsen, C. B. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)73945-3 · Cited by 223 · see citing works
Self-citationA lattice model for protein structure prediction at low resolution.
Hinds, D. A., & Levitt, M. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.7.2536 · Cited by 217 · see citing works
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Nussinov, R., Zhang, M., Liu, Y., & Jang, H. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c04346 · Cited by 190 · see citing works
Interactions by disorder – A matter of context
Bugge, K., Brakti, I., Fernandes, C. B., Dreier, J. E., Lundsgaard, J. E., Olsen, J. G., Skriver, K., & Kragelund, B. B. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00110 · Cited by 155 · see citing works
“…the importance of context in the understanding of proteins was formulated by Christian B. Anfinsen stating “ that the native conformation is determined by the totality of interatomic interactions and hence by the amino acid sequence, in a given environment ” (Anfinsen et al., 1961; Anfinsen, 1973).”
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Laurents, D. V. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.906437 · Cited by 95 · see citing works
Usmanova, D. R., Bogatyreva, N. S., Ariño Bernad, J., Eremina, A. A., Gorshkova, A. A., Kanevskiy, G. M., Lonishin, L. R., Meister, A. V., Yakupova, A. G., Kondrashov, F. A., et al. (2018) · Bioinformatics · doi:10.1093/bioinformatics/bty340 · Cited by 93 · see citing works
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Bouatta, N., Sorger, P., & AlQuraishi, M. (2021) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798321007531 · Cited by 69 · see citing works
Structural determinants of co-translational protein complex assembly
Mallik, S., Venezian, J., Lobov, A., Heidenreich, M., Garcia-Seisdedos, H., Yeates, T. O., Shiber, A., & Levy, E. D. (2025) · Cell · doi:10.1016/j.cell.2024.11.013 · Cited by 42 · see citing works
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Saldaño, T., Escobedo, N., Marchetti, J., Zea, D. J., Mac Donagh, J., Velez Rueda, A. J., Gonik, E., Melani, A. G., Novomisky Nechcoff, J., Salas, M. N., et al. (2021) · doi:10.1101/2021.10.27.466189 · Cited by 196 · see citing works
Decoding functional proteome information in model organisms using protein language models
Barrios-Núñez, I., Martínez-Redondo, G. I., Medina-Burgos, P., Cases, I., Fernández, R., & Rojas, A. M. (2024) · NAR Genomics and Bioinformatics · doi:10.1093/nargab/lqae078 · Cited by 13 · see citing works
Systematic characterization of indel variants using a yeast-based protein folding sensor
Larsen-Ledet, S., Lindemose, S., Panfilova, A., Gersing, S., Suhr, C. H., Genzor, A. V., Lanters, H., Nielsen, S. V., Lindorff-Larsen, K., Winther, J. R., et al. (2025) · Structure · doi:10.1016/j.str.2024.11.017 · Cited by 3 · see citing works
- Authors
- Anfinsen, C. B., Haber, E., Sela, M., & White, F. H.
- Affiliations
- National Institutes of Health (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1961-09
- Volume
- 47
- Issue
- 9
- Pages
- 1309-1314
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC223141
- OpenAlex
- W1991498388
- Cited by
- 1,182
- References
- 10
- Citations by year
- 2026: 19 · 2025: 38 · 2024: 33 · 2023: 36 · 2022: 54 · 2021: 35 · 2020: 40 · 2019: 36 · 2018: 26 · 2017: 25 · 2016: 36 · 2015: 29 · 2014: 40 · 2013: 38 · 2012: 47
- FWCI
- 7.03
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Profiles in Science (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- protein folding kinetics, protein oxidation, disulfide bond formation, protein refolding
- MeSH terms
- Kinetics, Oxidation-Reduction, Peptides, Physics, Ribonucleases
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