ArticleProceedings of the National Academy of Sciences of the United States of America2005
A protein folding pathway with multiple folding intermediates at atomic resolution.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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Who cites it
66 citing papers in PubMed.
- Heterogeneous folding landscapes and predetermined breaking points within a protein family.Protein science : a publication of the Protein Society · 2024Article
- Enzymatic and synthetic regulation of polypeptide folding.Chemical science · 2024Review
- Pathfinder: Protein folding pathway prediction based on conformational sampling.PLoS computational biology · 2023Article
- Cysteine-based protein folding modulators for trapping intermediates and misfolded forms.RSC advances · 2022Article
- Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophysical chemistry · 2022Review
- Effects of the Temperature and Salt Concentration on the Structural Characteristics of the Protein (PDB Code 1BBL).Polymers · 2022Article
- Article
- Conjecture on the Design of Helical Proteins.The journal of physical chemistry. B · 2020Article
- Unfolding cytochromes c-bJournal of inorganic biochemistry · 2020Article
- Funneled angle landscapes for helical proteins.Journal of inorganic biochemistry · 2020Article
- Effects of an Electric Field on the Conformational Transition of the Protein: A Molecular Dynamics Simulation Study.Polymers · 2019Article
- The case for defined protein folding pathways.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Protein Folding-How and Why: By Hydrogen Exchange, Fragment Separation, and Mass Spectrometry.Annual review of biophysics · 2016Review
- Cytochrome c folds through foldon-dependent native-like intermediates in an ordered pathway.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Cytochrome unfolding pathways from computational analysis of crystal structures.Journal of inorganic biochemistry · 2016Article
- Domain-swapped cytochromeChemical science · 2015Article
- Network representation of conformational transitions between hidden intermediates of Rd-apocytochrome b562.The Journal of chemical physics · 2015Article
- Statistical dictionaries for hypothetical in silico model of the early-stage intermediate in protein folding.Journal of computer-aided molecular design · 2015Article
- Some (dis)assembly required: partial unfolding in the Par-6 allosteric switch.Biophysical reviews · 2015Article
- Non-native structure appears in microseconds during the folding of E. coli RNase H.Journal of molecular biology · 2015Article
6 more citing papers are in PubMed but not listed here.
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3 authors.
Funding
Abstract
Using native-state hydrogen-exchange-directed protein engineering and multidimensional NMR, we determined the high-resolution structure (rms deviation, 1.1 angstroms) for an intermediate of the four-helix bundle protein: Rd-apocytochrome b562. The intermediate has the N-terminal helix and a part of the C-terminal helix unfolded. In earlier studies, we also solved the structures of two other folding intermediates for the same protein: one with the N-terminal helix alone unfolded and the other with a reorganized hydrophobic core. Together, these structures provide a description of a protein folding pathway with multiple intermediates at atomic resolution. The two general features for the intermediates are (i) native-like backbone topology and (ii) nonnative side-chain interactions. These results have implications for important issues in protein folding studies, including large-scale conformation search, -value analysis, and computer simulations.
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