The DOI matches its Crossref record.
Studies on the Reduction and Re-formation of Protein Disulfide Bonds
Open accessAbstract
The information contained in the amino acid sequence of a protein is linear, such as it is in DNA, but proteins function by virtue of the arrangement of their linear structure into a well-defined three-dimensional conformation. In this article, Anfinsen and Haber sought to determine how the two-dimensional data of DNA were translated into the three-dimensional information that was characteristic of globular proteins. This simple and elegant experiment was designed to determine what would happen when reduced, unfolded, and enzymatically inactive ribonuclease was allowed simply to refold in the presence of only neutral aqueous buffer and air. They found that most of the activity of the enzyme was regained.
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Cited by
ProtTrans: Toward Understanding the Language of Life Through Self-Supervised Learning
Elnaggar, A., Heinzinger, M., Dallago, C., Rehawi, G., Wang, Y., Jones, L., Gibbs, T., Feher, T., Angerer, C., Steinegger, M., et al. (2022) · IEEE Transactions on Pattern Analysis and Machine Intelligence · doi:10.1109/tpami.2021.3095381 · Cited by 2,329
THE KINETICS OF FORMATION OF NATIVE RIBONUCLEASE DURING OXIDATION OF THE REDUCED POLYPEPTIDE CHAIN
Anfinsen, C. B., Haber, E., Sela, M., & White, F. H. (1961) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.47.9.1309 · Cited by 1,182
Self-citationMerrifield, B. (1986) · Science · doi:10.1126/science.3961484 · Cited by 1,005
Beychok, S. (1966) · Science · doi:10.1126/science.154.3754.1288 · Cited by 375
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
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Metadata
- Authors
- Anfinsen, C. B., & Haber, E.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1961-05
- Volume
- 236
- Issue
- 5
- Pages
- 1361-1363
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W93532817
- Cited by
- 595
- References
- 0
- FWCI
- 16.71
- Type
- journal article
- Language
- en
- Open access
- hybrid
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