The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Direct observation of fast protein folding: the initial collapse of apomyoglobin.
Open accessAbstract
The rapid refolding dynamics of apomyoglobin are followed by a new temperature-jump fluorescence technique on a 15-ns to 0.5-ms time scale in vitro. The apparatus measures the protein-folding history in a single sweep in standard aqueous buffers. The earliest steps during folding to a compact state are observed and are complete in under 20 micros. Experiments on mutants and consideration of steady-state CD and fluorescence spectra indicate that the observed microsecond phase monitors assembly of an A x (H x G) helix subunit. Measurements at different viscosities indicate diffusive behavior even at low viscosities, in agreement with motions of a solvent-exposed protein during the initial collapse.
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Cites
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Formation of a Molten Globule Intermediate Early in the Kinetic Folding Pathway of Apomyoglobin
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Fast Events in Protein Folding: Helix Melting and Formation in a Small Peptide
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Cited by
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
Folding funnels, binding funnels, and protein function
Tsai, C., Kumar, S., Ma, B., & Nussinov, R. (1999) · Protein Science · doi:10.1110/ps.8.6.1181 · Cited by 648
The Levinthal paradox: yesterday and today
Karplus, M. (1997) · Folding and Design · doi:10.1016/s1359-0278(97)00067-9 · Cited by 264
Protein misfolding and aggregation in Alzheimer’s disease and type 2 diabetes mellitus
Ashraf, G., Greig, N., Khan, T., Hassan, I., Tabrez, S., Shakil, S., Sheikh, I., Zaidi, S., Akram, M., Jabir, N., et al. (2014) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527313666140917095514 · Cited by 236
Zhuang, W., Cui, R. Z., Silva, D.-A., & Huang, X. (2011) · The Journal of Physical Chemistry B · doi:10.1021/jp109592b · Cited by 70
Metadata
- Authors
- Ballew, R. M., Sabelko, J., & Gruebele, M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1996-06-11
- Volume
- 93
- Issue
- 12
- Pages
- 5759-5764
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1977470145
- Cited by
- 314
- References
- 24
- FWCI
- 12.99
- Type
- journal article
- Language
- en
- Open access
- green
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- Ballew, R. M., Sabelko, J., & Gruebele, M. (1996). Direct observation of fast protein folding: the initial collapse of apomyoglobin. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.93.12.5759
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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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