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Protein Sci. 1992 Jun;1(6):796-800.

Reversible dissociation and unfolding of the dimeric protein thymidylate synthase.

Author information

1
Department of Biochemistry and Biophysics, University of California, San Francisco 94143.

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.

PMID:
1304920
PMCID:
PMC2142238
DOI:
10.1002/pro.5560010611
[Indexed for MEDLINE]
Free PMC Article

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