Kinetic intermediates in the formation of the cytochrome c molten globule.
Abstract
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:
Submission Details
ID: n6Y3Ln2K3
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:34 p.m.
Version: 1
Publication Details
Colón W;Roder H,Nat. Struct. Biol. (1996) Kinetic intermediates in the formation of the cytochrome c molten globule. PMID:8946855Additional Information
Study Summary
| Number of data points | 18 |
| Proteins | Cytochrome c ; Cytochrome c |
| Unique complexes | 3 |
| 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 |
Structure view and single mutant data analysis
Study data
| Colors: | D | E | R | H | K | S | T | N | Q | A | V | I | L | M | F | Y | W | C | G | P |
|---|
Data Distribution
Studies with similar sequences (approximate matches)
Correlation with other assays (exact sequence matches)
Relevant UniProtKB Entries
| Percent Identity | Matching Chains | Protein | Accession | Entry Name |
|---|---|---|---|---|
| 100.0 | Cytochrome c | P00004 | CYC_HORSE | |
| 99.0 | Cytochrome c | P68097 | CYC_EQUAS | |
| 99.0 | Cytochrome c | P68096 | CYC_EQUBU | |
| 97.1 | Cytochrome c | P62894 | CYC_BOVIN | |
| 97.1 | Cytochrome c | P62895 | CYC_PIG | |
| 97.1 | Cytochrome c | P62896 | CYC_SHEEP | |
| 94.3 | Cytochrome c | P00007 | CYC_HIPAM | |
| 95.2 | Cytochrome c | P68099 | CYC_CAMDR | |
| 95.2 | Cytochrome c | P68100 | CYC_ESCRO | |
| 95.2 | Cytochrome c | P68098 | CYC_LAMGU | |
| 94.3 | Cytochrome c | P62897 | CYC_MOUSE | |
| 94.3 | Cytochrome c | P00008 | CYC_RABIT | |
| 94.3 | Cytochrome c | P62898 | CYC_RAT | |
| 94.3 | Cytochrome c | P00011 | CYC_CANLF | |
| 93.3 | Cytochrome c | P00014 | CYC_MACGI | |
| 93.3 | Cytochrome c | P00013 | CYC_MINSC | |
| 93.3 | Cytochrome c | Q52V09 | CYC_CEPBA | |
| 93.3 | Cytochrome c | P00012 | CYC_MIRLE | |
| 90.5 | Cytochrome c | Q52V10 | CYC_SAISC | |
| 92.3 | Cytochrome c | P81280 | CYC_ALLMI | |
| 92.2 | Cytochrome c | P00020 | CYC_ANAPL | |
| 91.3 | Cytochrome c | P00021 | CYC_COLLI | |
| 90.3 | Cytochrome c | B4USV4 | CYC_OTOGA |