ReviewInternational journal of molecular sciences2009
Early events, kinetic intermediates and the mechanism of protein folding in cytochrome C.
Review in International journal of molecular sciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
16 citing papers in PubMed, 33 citations in OpenAlex.
- Chlorogenic Acid Enhances the Chaperone Potential of BSA at Physiological Concentrations on Model Protein Cytochrome c.Cell biochemistry and biophysics · 2025Article
- Genetically Encoded Fluorescent Probe for Detection of Heme-Induced Conformational Changes in Cytochrome c.Biosensors · 2023Article
- Dramatic Shape Changes Occur as CytochromeThe journal of physical chemistry. B · 2020Article
- Heterogeneous folding and stretched kinetics.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Molten Globule, and Two-State vs. Non-Two-State Folding of Globular Proteins.Biomolecules · 2020Review
- Unified understanding of folding and binding mechanisms of globular and intrinsically disordered proteins.Biophysical reviews · 2018Review
- On the preservation of non-covalent protein complexes during electrospray ionization.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2016Article
- Heterogeneity of equilibrium molten globule state of cytochrome c induced by weak salt denaturants under physiological condition.PloS one · 2015Article
- Microsecond barrier-limited chain collapse observed by time-resolved FRET and SAXS.Journal of molecular biology · 2014Article
- Ultrafast hydrogen exchange reveals specific structural events during the initial stages of folding of cytochrome c.Journal of the American Chemical Society · 2014Article
- Proteins with highly similar native folds can show vastly dissimilar folding behavior when desolvated.Angewandte Chemie (International ed. in English) · 2014Article
- The role of key residues in structure, function, and stability of cytochrome-c.Cellular and molecular life sciences : CMLS · 2014Review
- Interconnection of salt-induced hydrophobic compaction and secondary structure formation depends on solution conditions: revisiting early events of protein folding at single molecule resolution.The Journal of biological chemistry · 2012Article
- Nanosecond time-resolved polarization spectroscopies: tools for probing protein reaction mechanisms.Methods (San Diego, Calif.) · 2010Article
- Role of protein stabilizers on the conformation of the unfolded state of cytochrome c and its early folding kinetics: investigation at single molecular resolution.The Journal of biological chemistry · 2010Article
- The human alpha-lactalbumin molten globule: comparison of structural preferences at pH 2 and pH 7.Journal of molecular biology · 2009Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Kinetic studies of the early events in cytochrome c folding are reviewed with a focus on the evidence for folding intermediates on the submillisecond timescale. Evidence from time-resolved absorption, circular dichroism, magnetic circular dichroism, fluorescence energy and electron transfer, small-angle X-ray scattering and amide hydrogen exchange studies on the t < or = 1 ms timescale reveals a picture of cytochrome c folding that starts with the approximately 1-micros conformational diffusion dynamics of the unfolded chains. A fractional population of the unfolded chains collapses on the 1 - 100 micros timescale to a compact intermediate I(C) containing some native-like secondary structure. Although the existence and nature of I(C) as a discrete folding intermediate remains controversial, there is extensive high time-resolution kinetic evidence for the rapid formation of I(C) as a true intermediate, i.e., a metastable state separated from the unfolded state by a discrete free energy barrier. Final folding to the native state takes place on millisecond and longer timescales, depending on the presence of kinetic traps such as heme misligation and proline mis-isomerization. The high folding rates observed in equilibrium molten globule models suggest that I(C) may be a productive folding intermediate. Whether it is an obligatory step on the pathway to the high free energy barrier associated with millisecond timescale folding to the native state, however, remains to be determined.
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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.