The 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. Study holds ProTherm entries: 7416, 7417, 7418, 7419, 7420, 7421, 7422, 7423, 14391 Extra Details:
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:34 p.m.
|Number of data points||18|
|Proteins||Cytochrome c ; Cytochrome c|
|Assays/Quantities/Protocols||Experimental Assay: ddG ; Experimental Assay: Tm ; Experimental Assay: dHvH ; Experimental Assay: Cm ; Experimental Assay: dG_H2O ; Experimental Assay: Cm ; Experimental Assay: dG_H2O ; Derived Quantity: dTm|
|Libraries||Mutations for sequence GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE|