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Cytochrome c folding pathway: kinetic native-state hydrogen exchange.
Proc Natl Acad Sci U S A. 2002 Sep 17;99(19):12173-8. doi: 10.1073/pnas.152439199. Epub 2002 Aug 26.
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Folding of horse cytochrome c in the reduced state.
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Evidence for an unfolding and refolding pathway in cytochrome c.
Nat Struct Biol. 1998 Sep;5(9):774-8. doi: 10.1038/1810.
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Kinetic mechanism of folding and unfolding of Rhodobacter capsulatus cytochrome c2.
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How cytochrome c folds, and why: submolecular foldon units and their stepwise sequential stabilization.
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Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands.
Biochemistry. 1994 Jun 7;33(22):6925-35. doi: 10.1021/bi00188a023.

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How to Turn an Electron Transfer Protein into a Redox Enzyme for Biosensing.
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POPPeT: a New Method to Predict the Protection Factor of Backbone Amide Hydrogens.
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The K79G Mutation Reshapes the Heme Crevice and Alters Redox Properties of Cytochrome c.
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The case for defined protein folding pathways.
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How cooperative are protein folding and unfolding transitions?
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Cytochrome c folds through foldon-dependent native-like intermediates in an ordered pathway.
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Highly polarized C-terminal transition state of the leucine-rich repeat domain of PP32 is governed by local stability.
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