ArticleProceedings of the National Academy of Sciences of the United States of America2009
Folding energy landscape of cytochrome cb562.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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
10 citing papers in PubMed.
- Unfolding cytochromes c-bJournal of inorganic biochemistry · 2020Article
- Funneled angle landscapes for helical proteins.Journal of inorganic biochemistry · 2020Article
- Domain-swapped cytochromeChemical science · 2015Article
- Fast protein folding kinetics.Quarterly reviews of biophysics · 2014Review
- Intrachain contact dynamics in unfolded cytochrome cb562.The journal of physical chemistry. B · 2013Article
- Snapshots of a protein folding intermediate.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Fusion partner toolchest for the stabilization and crystallization of G protein-coupled receptors.Structure (London, England : 1993) · 2012Article
- 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
- Direct visualization reveals dynamics of a transient intermediate during protein assembly.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Fluorescence anisotropy and resonance energy transfer: powerful tools for measuring real time protein dynamics in a physiological environment.Current opinion in pharmacology · 2010Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Cytochrome cb(562) is a variant of an Escherichia coli four-helix bundle b-type heme protein in which the porphyrin prosthetic group is covalently ligated to the polypeptide near the terminus of helix 4. Studies from other laboratories have shown that the apoprotein folds rapidly without the formation of intermediates, whereas the holoprotein loses heme before native structure can be attained. Time-resolved fluorescence energy transfer (TRFET) measurements of cytochrome cb(562) refolding triggered using an ultrafast continuous-flow mixer (150 micros dead time) reveal that heme attachment to the polypeptide does not interfere with rapid formation of the native structure. Analyses of the TRFET data produce distributions of Trp-59-heme distances in the protein before, during, and after refolding. Characterization of the moments and time evolution of these distributions provides compelling evidence for a refolding mechanism that does not involve significant populations of intermediates. These observations suggest that the cytochrome b(562) folding energy landscape is minimally frustrated and able to tolerate the introduction of substantial perturbations (i.e., the heme prosthetic group) without the formation of deep misfolded traps.
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Registered trials
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