Reversible dissociation and unfolding of the dimeric protein thymidylate synthase.
Abstract
Conditions for in vitro unfolding and refolding of dimeric thymidylate synthase from Lactobacillus casei were found. Ultraviolet difference and circular dichroism spectra showed that the enzyme was completely unfolded at concentrations of urea over 5.5 M. As measured by restoration of enzyme activity, refolding was accomplished when 0.5 M potassium chloride was included in the refolding mixture. Recombination of subunits from catalytically inactive mutant homodimers to form an active hybrid dimer was achieved under these unfolding-refolding conditions, demonstrating a monomer to dimer association step. Study holds ProTherm entries: 10382 Extra Details: additive : EDTA(0.1 mM), dimerization; folding; oligomerization; thymidylate synthase
Submission Details
ID: fw7pNpXU3
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:40 p.m.
Version: 1
Publication Details
Perry KM;Pookanjanatavip M;Zhao J;Santi DV;Stroud RM,Protein Sci. (1992) Reversible dissociation and unfolding of the dimeric protein thymidylate synthase. PMID:1304920Additional Information
Study Summary
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 |
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Data Distribution
Studies with similar sequences (approximate matches)