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
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:22 p.m.
|Number of data points||3|
|Proteins||Glutaredoxin ; Glutaredoxin|
|Assays/Quantities/Protocols||Experimental Assay: dG ; Experimental Assay: dG|
|Libraries||Mutations for sequence MFKVYGYDSNIHKCVYCDNAKRLLTVKKQPFEFINIMPEKGVFDDEKIAELLTKLGRDTQIGLTMPQVFAPDGSHIGGFDQLREYFK|
|Percent Identity||Matching Chains||Protein||Accession||Entry Name|