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Nucleation, Rapid Folding, and Globular Intrachain Regions in Proteins
Open accessAbstract
Distinct structural regions have been found in several globular proteins composed of single polypeptide chains. The existence of such regions and the continuity of peptide chain within them, coupled with kinetic arguments, suggests that the early stages of three-dimensional structure formation (nucleation) occur independently in separate parts of these molecules. A nucleus can grow rapidly by adding peptide chain segments that are close to the nucleus in aminoacid sequence. Such a process would generate three-dimensional (native) protein structures that contain separate regions of continuous peptide chain. Possible means of testing this hypothesis are discussed.
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Cited by
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
Nucleation mechanisms in protein folding
Fersht, A. R. (1997) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(97)80002-4 · Cited by 545
Human apolipoprotein E3 in aqueous solution. I. Evidence for two structural domains.
Wetterau, J. R., Aggerbeck, L. P., Rall, S. C., & Weisgraber, K. H. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68778-2 · Cited by 293
A 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
Merizo: a rapid and accurate protein domain segmentation method using invariant point attention
Lau, A. M., Kandathil, S. M., & Jones, D. T. (2023) · Nature Communications · doi:10.1038/s41467-023-43934-4 · Cited by 48
Metadata
- Authors
- Wetlaufer, D. B.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1973-03
- Volume
- 70
- Issue
- 3
- Pages
- 697-701
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2055118532
- Cited by
- 831
- References
- 0
- FWCI
- 7.30
- Type
- journal article
- Language
- en
- Open access
- green
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