Structural differences between oxidized and reduced thioredoxin monitored by two-dimensional 1H NMR spectroscopy. H.J. Dyson, A. Holmgren, & P.E. Wright (1988) FEBS Lett. 228, 254-258.
Assignment of the proton NMR spectrum of reduced and oxidized thioredoxin: sequence-specific assignments, secondary structure and global fold. H.J. Dyson, A. Holmgren, & P.E. Wright (1989) Biochemistry 28, 7074-7087.
Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy. H.J. Dyson, G.P. Gippert, D.A. Case, A. Holmgren, & P.E. Wright (1990) Biochemistry 29, 4129-4136.
Proton-transfer effects in the active-site region of Escherichia coli thioredoxin using two-dimensional 1H NMR. H.J. Dyson, L.L. Tennant, & A. Holmgren (1991) Biochemistry 30, 4262-4268.
Assignment of the 15N NMR spectrum of reduced and oxidized Escherichia coli thioredoxin. K. Chandrasekhar, G. Krause, A. Holmgren, & H.J. Dyson (1991) FEBS Lett. 284, 178-183.
Comparison of backbone and tryptophan side-chain dynamics of reduced and oxidized Escherichia coli thioredoxin using 15N NMR relaxation measurements. M.J. Stone, K. Chandrasekhar, A. Holmgren, P.E. Wright, & H.J. Dyson (1993) Biochemistry 32, 426-435.
Characterization by 1H NMR of a C32S,C35S double mutant of Escherichia coli thioredoxin confirms its resemblance to the reduced wild-type protein. H.J. Dyson, M.-F. Jeng, P. Model, & A. Holmgren (1994) FEBS Lett. 339, 11-17.
Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin. K. Chandrasekhar, A.P. Campbell, M.-F. Jeng, A. Holmgren, & H.J. Dyson (1994) J. Biomol. NMR 4, 411-432.
High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin. M.-F. Jeng, A.P. Campbell, T. Begley, A. Holmgren, D.A. Case, P.E. Wright, & H.J. Dyson (1994) Structure 2, 853-868.
Comparison of the hydrogen exchange behavior of reduced and oxidized Escherichia coli thioredoxin. M.-F. Jeng & H.J. Dyson (1995) Biochemistry 34, 611-619.
Proton sharing between cysteine thiols in Escherichia coli thioredoxin: implications for the mechanism of reduction of protein disulfides. M.-F. Jeng, A. Holmgren, & H.J. Dyson (1995) Biochemistry 34, 10101-10105.
Direct measurement of the Asp-26 pKa for reduced Escherichia coli thioredoxin by 13C NMR. M.-F. Jeng and H. J. Dyson (1996) Biochemistry 35, 1-6.
Replacement of Trp-28 in Escherichia coli thioredoxin by site-directed mutagenesis affects thermodynamic stability but not function. I. Slaby, V. Cerna, M.-F. Jeng, H.J. Dyson and A. Holmgren (1996) J. Biol. Chem. 271, 3091-3096.
Effects of buried charged
groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin:
Structural and functional characterization of mutants of Asp 26 and Lys
57. H.J. Dyson, M.-F. Jeng, L.L. Tennant,
Calculations of electrostatic interactions and pKas in the active site of Escherichia coli thioredoxin. V. Dillet, H.J. Dyson and D. Bashford (1998) Biochemistry 37, 10298-10306.
NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and a covalent thioredoxin-peptide complex. M.-F. Jeng, M.T. Reymond, L.L. Tennant, A. Holmgren and H.J. Dyson (1998). Eur. J. Biochem. 257, 299-308.
Assignment of 1H, 13C and 15N resonances of reduced Escherichia coli glutaredoxin 2. B. Xia, J. Chung, A. Vlamis-Gardikas, A. Holmgren, P.E. Wright and H.J. Dyson (1999) J. Biomol. NMR 14, 197-198.
Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases. B. Xia, A. Vlamis-Gardikas, A. Holmgren, P.E. Wright and H.J. Dyson (2001) J. Mol. Biol. 310, 907-918.