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The refolding kinetics of the tryptophan synthase β 2 subunit have been investigated by circular dichroism (CD) and binding of a fluorescent hydrophobic probe (ANS), using the stopped-flow technique. The kinetics of regain of the native far UV CD signal show that, upon refolding of urea denatured β 2 , more than half of the protein secondary structure is formed within the dead time...
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