The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering
Open accessAbstract
Time-resolved small-angle x-ray scattering was used to measure the radius of gyration of cytochrome c after initiation of folding by a pH jump. Submillisecond time resolution was obtained with a microfabricated diffusional mixer and synchrotron radiation. The results show that the protein first collapses to compact denatured structures before folding very fast to the native state.
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Citations
Cites
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THEORY OF PROTEIN FOLDING: The Energy Landscape Perspective
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Molecular-weight Determination by Light Scattering.
Debye, P. (1947) · The Journal of Physical and Colloid Chemistry · doi:10.1021/j150451a002 · Cited by 1,231
Hydrodynamic Focusing on a Silicon Chip: Mixing Nanoliters in Microseconds
Knight, J. B., Vishwanath, A., Brody, J. P., & Austin, R. H. (1998) · Physical Review Letters · doi:10.1103/physrevlett.80.3863 · Cited by 887
Self-citationHow do small single-domain proteins fold?
Jackson, S. E. (1998) · Folding and Design · doi:10.1016/s1359-0278(98)00033-9 · Cited by 880
Diffusive dynamics of the reaction coordinate for protein folding funnels
Socci, N. D., Onuchic, J. N., & Wolynes, P. G. (1996) · The Journal of Chemical Physics · doi:10.1063/1.471317 · Cited by 475
Protein folding in the landscape perspective: Chevron plots and non-arrhenius kinetics
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The barriers in protein folding
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Self-citationKinetic Mechanism of Cytochrome c Folding: Involvement of the Heme and Its Ligands
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Cited by
Small-angle scattering studies of biological macromolecules in solution
Svergun, D. I., & Koch, M. H. J. (2003) · Reports on Progress in Physics · doi:10.1088/0034-4885/66/10/r05 · Cited by 1,014
Millisecond Kinetics on a Microfluidic Chip Using Nanoliters of Reagents
Song, H., & Ismagilov, R. F. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0354566 · Cited by 693
Deniz, A. A., Laurence, T. A., Beligere, G. S., Dahan, M., Martin, A. B., Chemla, D. S., Dawson, P. E., Schultz, P. G., & Weiss, S. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.090104997 · Cited by 469
Small-Angle X-ray Scattering of Polymers
Chu, B., & Hsiao, B. S. (2001) · Chemical Reviews · doi:10.1021/cr9900376 · Cited by 455
Single-Molecule Measurement of Protein Folding Kinetics
Lipman, E. A., Schuler, B., Bakajin, O., & Eaton, W. A. (2003) · Science · doi:10.1126/science.1085399 · Cited by 401
Self-citation
Metadata
- Authors
- Pollack, L., Tate, M. W., Darnton, N. C., Knight, J. B., Gruner, S. M., Eaton, W. A., & Austin, R. H.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1999-08-31
- Volume
- 96
- Issue
- 18
- Pages
- 10115-10117
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2154916820
- Cited by
- 285
- References
- 20
- FWCI
- 5.00
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering. https://app.cochat.ai/papers/10.1073/pnas.96.18.10115
- The paper
- Pollack, L., Tate, M. W., Darnton, N. C., Knight, J. B., Gruner, S. M., Eaton, W. A., & Austin, R. H. (1999). Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.96.18.10115
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.
