The equilibrium unfolding transition of class pi glutathione S-transferase, a homodimeric protein, from porcine lung was monitored by spectroscopic methods (fluorescence emission and ultraviolet absorption), and by enzyme activity changes. Solvent (guanidine hydrochloride and urea)-induced denaturation is well described by a two-state model involving significant populations of only the folded dimer and unfolded monomer. Neither a folded, active monomeric form nor stable unfolding intermediates were detected. The conformational stability, delta Gu (H2O), of the native dimer was estimated to be about 25.3 +/- 2 kcal/mol at 20 degrees C and pH6.5. Study holds ProTherm entries: 7612, 7613 Extra Details: additive : EDTA(1 mM),NaN3(0.02%) was added in the experiment homodimeric protein; enzyme activity; two-state model;,conformational stability
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:34 p.m.
|Number of data points||4|
|Proteins||Glutathione S-transferase omega-1|
|Assays/Quantities/Protocols||Experimental Assay: m ; Experimental Assay: dG_H2O ; Experimental Assay: m ; Experimental Assay: dG_H2O|
|Libraries||Mutations for sequence MSGGSARSLGKGSAPPGPVPEGLIRVYSMRFCPFAQRTLLVLNAKGIRHQVININLKNKPEWFFQKNPSGLVPVLENSQGQLIYESAITCEYLDEAYPGKKLLPDDPYEKACQKMVFELSSKVPPLLIRFIRRENEADCSGLKEELRKEFSKLEEVLTKKKTTYFGGSSLSMIDYLIWPWFERLEALELNECIDHTPKLKLWMAAMMKDPAVSALHIEPRDLRAFNDLYLQNSPEACDYGL|