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Colon W , Roder H
Kinetic intermediates in the formation of the cytochrome c molten globule
Nature Structural Biology. 1996 Dec;3(12) :1019-1025
AbstractThe relationship between molten globules and transient intermediates in protein folding has been explored by equilibrium and kinetic analysis of the compact acid-denatured A-state of cytochrome c. The chloride-induced formation of the A-state is a complex reaction with structural intermediates resembling those found under native refolding conditions, including a rapidly formed compact state and a subsequent intermediate with interacting N- and C-terminal helices. Together with mutational evidence for specific helix-helix packing interactions, this shows that the A-state is a stable analogue of a late folding intermediate. The L94A mutation blocks all folding steps after the initial collapse and its equilibrium state resembles early kinetic intermediates.
NotesTimes Cited: 33 English Article VW079 NATURE STRUCT BIOLOGY