The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Fast events in protein folding initiated by nanosecond laser photolysis.
Open accessAbstract
Initiation of protein folding by light can dramatically improve the time resolution of kinetic studies. Here we present an example of an optically triggered folding reaction by using nanosecond photodissociation of the heme-carbon monoxide complex of reduced cytochrome c. The optical trigger is based on the observation that under destabilizing conditions cytochrome c can be unfolded by preferential binding of carbon monoxide to the covalently attached heme group in the unfolded state. Photodissociation of the carbon monoxide thus triggers the folding reaction. We used time-resolved absorption spectroscopy to monitor binding at the heme. Before folding begins we observe transient binding of both nonnative and native ligands from the unfolded polypeptide on a microsecond time scale. Kinetic modeling suggests that the intramolecular binding of methionine-65 and -80 is faster than that of histidine-26 and -33, even though the histidines are closer to the heme. This optical trigger should provide a powerful method for studying chain collapse and secondary structure formation in cytochrome c without any limitations in time resolution.
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Cites
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Kuwajima, K. (1989) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340060202 · Cited by 1,439
INTERMEDIATES IN THE FOLDING REACTIONS OF SMALL PROTEINS
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Self-citationThe Role of Solvent Viscosity in the Dynamics of Protein Conformational Changes
Ansari, A., Jones, C. M., Henry, E. R., Hofrichter, J., & Eaton, W. A. (1992) · Science · doi:10.1126/science.1615323 · Cited by 550
Self-citationCreighton, T. E. (1990) · Biochemical Journal · doi:10.1042/bj2700001 · Cited by 515
Rate Theories and Puzzles of Hemeprotein Kinetics
Frauenfelder, H., & Wolynes, P. G. (1985) · Science · doi:10.1126/science.4012322 · Cited by 488
Cooperativity in protein-folding kinetics.
Dill, K. A., Fiebig, K. M., & Chan, H. S. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.5.1942 · Cited by 480
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Cited by
Funnels, pathways, and the energy landscape of protein folding: A synthesis
Bryngelson, J. D., Onuchic, J. N., Socci, N. D., & Wolynes, P. G. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340210302 · Cited by 2,648
“Also, multi-exponential decay of relaxation properties are seen in these early events [61].”
BackgroundFrom 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
THEORY OF PROTEIN FOLDING: The Energy Landscape Perspective
Onuchic, J. N., Luthey-Schulten, Z., & Wolynes, P. G. (1997) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.48.1.545 · Cited by 2,210
Toward an outline of the topography of a realistic protein-folding funnel.
Onuchic, J. N., Wolynes, P. G., Luthey-Schulten, Z., & Socci, N. D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.8.3626 · Cited by 523
Kinetics of protein folding: Nucleation mechanism, time scales, and pathways
Guo, Z., & Thirumalai, D. (1995) · Biopolymers · doi:10.1002/bip.360360108 · Cited by 339
Metadata
- Authors
- Jones, C. M., Henry, E. R., Hu, Y., Chan, C. K., Luck, S. D., Bhuyan, A., Roder, H., Hofrichter, J., & Eaton, W. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1993-12-15
- Volume
- 90
- Issue
- 24
- Pages
- 11860-11864
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1997805535
- Cited by
- 306
- References
- 17
- FWCI
- 4.25
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Jones, C. M., Henry, E. R., Hu, Y., Chan, C. K., Luck, S. D., Bhuyan, A., Roder, H., Hofrichter, J., & Eaton, W. A. (1993). Fast events in protein folding initiated by nanosecond laser photolysis. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.90.24.11860
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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).
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