The DOI matches its Crossref record.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
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
CASP13 target classification into tertiary structure prediction categories
Kinch, L. N., Kryshtafovych, A., Monastyrskyy, B., & Grishin, N. V. (2019) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25775 · Cited by 36
Janin, J., & Wodak, S. J. (2002) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(02)61000-9 · Cited by 31
Protein intrinsically disordered regions have a non-random, modular architecture
McConnell, B. S., & Parker, M. W. (2023) · Bioinformatics · doi:10.1093/bioinformatics/btad732 · Cited by 17
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
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 ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
