ArticleProceedings of the National Academy of Sciences of the United States of America2007
Site-specific collapse dynamics guide the formation of the cytochrome c' four-helix bundle.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
12 citing papers in PubMed, 31 citations in OpenAlex.
- Kinetics of protein-assisted nucleic acid interconversion monitored by transient time resolved fluorescence in microfluidic droplets.Nucleic acids research · 2021Article
- Advances in turbulent mixing techniques to study microsecond protein folding reactions.Biopolymers · 2013Article
- Intrachain contact dynamics in unfolded cytochrome cb562.The journal of physical chemistry. B · 2013Article
- The loop hypothesis: contribution of early formed specific non-local interactions to the determination of protein folding pathways.Biophysical reviews · 2013Review
- Snapshots of a protein folding intermediate.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- How, when and why proteins collapse: the relation to folding.Current opinion in structural biology · 2012Review
- Charge photoinjection in intercalated and covalently bound [Re(CO)3(dppz)(py)]+-DNA constructs monitored by time-resolved visible and infrared spectroscopy.Journal of the American Chemical Society · 2011Article
- Manifestations of native topology in the denatured state ensemble of Rhodopseudomonas palustris cytochrome c'.Biochemistry · 2011Article
- Folding energy landscape of cytochrome cb562.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Collapse transition in proteins.Physical chemistry chemical physics : PCCP · 2009Article
- Microsecond acquisition of heterogeneous structure in the folding of a TIM barrel protein.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Probing the cytochrome c' folding landscape.Journal of inorganic biochemistry · 2007Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The evolution of tryptophan-to-heme (W/heme) distance distributions extracted from analysis of fluorescence energy transfer kinetics during the refolding of Rhodopseudomonas palustris cytochrome c' reveals dramatic differences between two variants [W32 (Q1A/F32W/W72F) and W72 (Q1A)]. Both W32/heme and W72/heme distance distributions measured at the earliest time point attainable with a continuous-flow mixer (150 mus) confirm that the polypeptide ensemble is not uniformly collapsed and that native structure is not formed. Time-resolved fluorescence spectra indicate that W32 is sequestered from the aqueous solution during the first 700 mus of folding, whereas W72 remains exposed to solvent. The first moment of the W32/heme distance distribution evolves to its native value faster than that of W72, suggesting that the approach of W32 to the heme precedes that of W72.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.