Authors:
Zitzewitz, JA
Ibarra-Molero, B
Fishel, DR
Terry, KL
Matthews, CR
Citation: Ja. Zitzewitz et al., Preformed secondary structure drives the association reaction of GCN4-p1, a model coiled-coil system, J MOL BIOL, 296(4), 2000, pp. 1105-1116
Authors:
Zitzewitz, JA
Gualfetti, PJ
Perkons, IA
Wasta, SA
Matthews, CR
Citation: Ja. Zitzewitz et al., Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein, PROTEIN SCI, 8(6), 1999, pp. 1200-1209
Authors:
Gualfetti, PJ
Iwakura, M
Lee, JC
Kihara, H
Bilsel, O
Zitzewitz, JA
Matthews, CR
Citation: Pj. Gualfetti et al., Apparent radii of the native, stable intermediates and unfolded conformersof the alpha-subunit of tryptophan synthase from E-coli, a TIM barrel protein, BIOCHEM, 38(40), 1999, pp. 13367-13378
Citation: Ja. Zitzewitz et Cr. Matthews, Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: An amino-terminal autonomous folding unit controls severalrate-limiting steps in the folding of a single domain protein, BIOCHEM, 38(31), 1999, pp. 10205-10214
Authors:
Bilsel, O
Zitzewitz, JA
Bowers, KE
Matthews, CR
Citation: O. Bilsel et al., Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: Global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels, BIOCHEM, 38(3), 1999, pp. 1018-1029
Authors:
Bilsel, O
Yang, L
Zitzewitz, JA
Beechem, JM
Matthews, CR
Citation: O. Bilsel et al., Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time, BIOCHEM, 38(13), 1999, pp. 4177-4187