Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR.

Por Jones, B. E., Matthews, C. R.
Publicado em 1995

The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli.

Por Gualfetti, P. J., Bilsel, O., Matthews, C. R.
Publicado em 1999

Tryptophan replacements in the trp aporepressor from Escherichia coli: probing the equilibrium and kinetic folding models.

Por Mann, C. J., Royer, C. A., Matthews, C. R.
Publicado em 1993

Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants.

Por Royer, C. A., Mann, C. J., Matthews, C. R.
Publicado em 1993

Probing minimal independent folding units in dihydrofolate reductase by molecular dissection.

Por Gegg, C. V., Bowers, K. E., Matthews, C. R.
Publicado em 1997

Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein.

Por Zitzewitz, J. A., Gualfetti, P. J., Perkons, I. A., Wasta, S. A., Matthews, C. R.
Publicado em 1999