Folding kinetics of phage T4 thioredoxin.
Abstract
The folding mechanism for bacteriophage T4 thioredoxin is best described by a four-state box mechanism, N----Uc----Ut----It----N, where N indicates native, Uc the unfolded form with the cis proline isomer, Ut unfolded with the trans proline isomer, and It a compact form with a trans proline isomer. Both manual mixing fluorescence and size-exclusion chromatography indicate that there is a cis-trans proline isomerization that is important to the folding pathway. Furthermore, the data suggest that the cis-trans isomerization can also occur in a compact nativelike state which is referred to as It. The slow phase seen in fluorescence seems to be monitoring the cis-trans isomerization in the compact form, not the isomerization which occurs in the denatured state. Study holds ProTherm entries: 3667, 3668, 3669 Extra Details: measurements were made at far UV four-state box mechanism; fluorescence;,size-exclusion chromatography; cis-trans isomerization
Submission Details
ID: GFdkYHxG4
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:22 p.m.
Version: 1
Publication Details
Borden KL;Richards FM,Biochemistry (1990) Folding kinetics of phage T4 thioredoxin. PMID:2186806Additional Information
Study Summary
| Number of data points | 3 |
| Proteins | Glutaredoxin ; Glutaredoxin |
| Unique complexes | 1 |
| Assays/Quantities/Protocols | Experimental Assay: dG ; Experimental Assay: dG |
| Libraries | Mutations for sequence MFKVYGYDSNIHKCVYCDNAKRLLTVKKQPFEFINIMPEKGVFDDEKIAELLTKLGRDTQIGLTMPQVFAPDGSHIGGFDQLREYFK |
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 | Glutaredoxin | P00276 | GLRX_BPT4 |