The DOI matches its Crossref record.
Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probe
Abstract
Binding of the hydrophobia fluorescent probe, 1‐anilino‐naphthalene‐8‐sulfonate (ANS), to synthetic polypeptides and proteins with a different structural organization has been studied. It has been shown that ANS has a much stronger affinity to the protein “molten globule” state, with a pronounced secondary structure and compactness, but without a tightly packed tertiary structure as compared with its affinity to the native and coil‐like proteins, or to coil‐like, α‐helical, or β‐structural hydrophilic homopolypeptides. The possibility of using ANS for the study of equilibrium and kinetic molten globule intermediates is demonstrated, with carbonic anhydrase, β‐lactamase, and α‐lactalbumin as examples.
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
Metal-triggered Structural Transformations, Aggregation, and Fibrillation of Human α-Synuclein
Uversky, V. N., Li, J., & Fink, A. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105343200 · Cited by 1,103
Self-citationEvidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation
Uversky, V. N., Li, J., & Fink, A. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010907200 · Cited by 1,096
Self-citationUnderstanding how proteins fold: the lysozyme story so far
Dobson, C. M., Evans, P. A., & Radford, S. E. (1994) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(94)90171-6 · Cited by 340
Jeganathan, S., von Bergen, M., Mandelkow, E.-M., & Mandelkow, E. (2008) · Biochemistry · doi:10.1021/bi800783d · Cited by 286
A Buried Polar Interaction Imparts Structural Uniqueness in a Designed Heterodimeric Coiled Coil
Lumb, K. J., & Kim, P. S. (1995) · Biochemistry · doi:10.1021/bi00027a013 · Cited by 266
Metadata
- Authors
- Semisotnov, G. V., Rodionova, N. A., Razgulyaev, O. I., Uversky, V. N., Gripas', A. F., & Gilmanshin, R. I.
- Venue
- Biopolymers
- Publisher
- Wiley
- Published
- 1991-01
- Volume
- 31
- Issue
- 1
- Pages
- 119-128
- ISSN
- 0006-3525 (ISSN-L)
- 1097-0282
- OpenAlex
- W2145538573
- Cited by
- 1,269
- References
- 0
- FWCI
- 6.85
- Type
- journal article
- Language
- en
- Open access
- closed
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probe. https://app.cochat.ai/papers/10.1002/bip.360310111
- The paper
- Semisotnov, G. V., Rodionova, N. A., Razgulyaev, O. I., Uversky, V. N., Gripas', A. F., & Gilmanshin, R. I. (1991). Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers. https://doi.org/10.1002/bip.360310111
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.
