NMR evidence for the stepwise unfolding of the two domains of tryptophan synthase α-subunit

An active proteolytic derivative of the .alpha. subunit of tryptophan synthase. Identification of the site of cleavage and characterization of the fragments

1979 • 112 citations

Urea-induced unfolding of the .alpha. subunit of tryptophan synthase: evidence for a multistate process

1981 • 109 citations

Guanidine hydrochloride-induced unfolding of the .alpha. subunit of tryptophan synthase and of the two .alpha. proteolytic fragments: evidence for stepwise unfolding of the two .alpha. domains

1982 • 88 citations

Characterization of the slow steps in the folding of the .alpha. subunit of tryptophan synthase

1981 • 54 citations

Comparison of Denaturation by Guanidine Hydrochloride of the Wild Type Tryptophan Synthase α-Subunit of Escherichia coli and Two Mutant Proteins (Glu 49—Met or Gln)

1979 • 53 citations

pH dependence of stability of the wild-type tryptophan synthase α-subunit and two mutant proteins (Glu49 → Met or Gln)

1980 • 45 citations