Folding kinetics of phage T4 thioredoxin.
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.
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511.
K L
KL
Borden
F M
FM
Richards
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D002942:Circular Dichroism; D004926:Escherichia coli / Q000378:metabolism; D007700:Kinetics; D008962:Models, Theoretical; D008969:Molecular Sequence Data; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013604:T-Phages / Q000378:metabolism*; D013816:Thermodynamics; D013879:Thioredoxins / Q000378:metabolism*
D001426:Bacterial Proteins; D013879:Thioredoxins