As a prelude to complete structure calculations of both the oxidized and reduced forms of Escherichia coli thioredoxin (M(r) 11,700), we have analyzed the NMR data obtained for the two proteins under identical conditions. The complete aliphatic 13C assignments for both oxidized and reduced thioredoxin are reported. Correlations previously noted between 13C chemical shifts and secondary structure are confirmed in this work, and significant differences are observed in the C beta and C gamma shifts between cis- and trans-proline, consistent with previous work that identifies this as a simple and unambiguous method of identifying cis-proline residues in proteins. Reduction of the disulfide bond in the active-site Cys32-Gly-Pro-Cys35 sequence causes changes in the 1H, 15N and 13C chemical shifts of residues close to the active site, some of them quite far distant in the amino acid sequence. Coupling constants, both backbone and side chain, show some differences between the two proteins, and the NOE connectivities and chemical shifts are consistent with small changes in the positions of several side chains, including the two tryptophan rings (Trp28 and Trp31). These results show that, consistent with the biochemical behavior of thioredoxin, there are minimal differences in backbone configuration between the oxidized and reduced forms of the protein.
[NMR paper] NMR studies of the aggregation of glucagon-like peptide-1: formation of a symmetric h
NMR studies of the aggregation of glucagon-like peptide-1: formation of a symmetric helical dimer.
Related Articles NMR studies of the aggregation of glucagon-like peptide-1: formation of a symmetric helical dimer.
FEBS Lett. 2002 Mar 27;515(1-3):165-70
Authors: Chang X, Keller D, O'Donoghue SI, Led JJ
Nuclear magnetic resonance (NMR) spectroscopy reveals that higher-order aggregates of glucagon-like peptide-1-(7-36)-amide (GLP-1) in pure water at pH 2.5 are disrupted by 35% 2,2,2-trifluoroethanol (TFE), and form a stable and highly symmetric...
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[NMR paper] 13C NMR chemical shifts can predict disulfide bond formation.
13C NMR chemical shifts can predict disulfide bond formation.
Related Articles 13C NMR chemical shifts can predict disulfide bond formation.
J Biomol NMR. 2000 Oct;18(2):165-71
Authors: Sharma D, Rajarathnam K
The presence of disulfide bonds can be detected unambiguously only by X-ray crystallography, and otherwise must be inferred by chemical methods. In this study we demonstrate that 13C NMR chemical shifts are diagnostic of disulfide bond formation, and can discriminate between cysteine in the reduced (free) and oxidized (disulfide bonded)...
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11-19-2010 08:29 PM
[NMR paper] Novel mechanism of surface catalysis of protein adduct formation. NMR studies of the
Novel mechanism of surface catalysis of protein adduct formation. NMR studies of the acetylation of ubiquitin.
Related Articles Novel mechanism of surface catalysis of protein adduct formation. NMR studies of the acetylation of ubiquitin.
J Biol Chem. 2000 Oct 13;275(41):31908-13
Authors: Macdonald JM, Haas AL, London RE
Reactivity of surface lysyl residues of proteins with a broad range of chemical agents has been proposed to be dependent on the catalytic microenvironment of the residue. We have investigated the acetylation of wild type...
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[NMR paper] 1H-NMR and raman studies on perforating trauma-induced cataract formation in a mouse
1H-NMR and raman studies on perforating trauma-induced cataract formation in a mouse lens.
Related Articles 1H-NMR and raman studies on perforating trauma-induced cataract formation in a mouse lens.
Biochim Biophys Acta. 2000 Mar 6;1474(1):23-30
Authors: Nakamura K, Jung YM, Era S, Sogami M, Ozaki Y, Takasaki A
In order to provide new insight into the molecular mechanism of perforating trauma-induced cataract formation in an 8-week-old ddY mouse lens, we performed an in situ investigation into changes in the water-protein and/or...
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[NMR paper] NMR and luminescence studies on the formation of ternary adducts between HSA and Ln(I
NMR and luminescence studies on the formation of ternary adducts between HSA and Ln(III)-malonate complexes.
Related Articles NMR and luminescence studies on the formation of ternary adducts between HSA and Ln(III)-malonate complexes.
Biochim Biophys Acta. 1998 Jun 11;1385(1):7-16
Authors: Aime S, Bettinelli M, Ferrari M, Razzano E, Terreno E
At physiological pH and in the presence of an excess of malonate ligand (MAL), the lanthanide ions (Ln=Eu(III), Gd(III) and Tb(III)) are under the form of -. Upon addition of human serum albumin (HSA),...
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[NMR paper] Thiol/disulfide formation associated with the redox activity of the [Fe3S4] cluster o
Thiol/disulfide formation associated with the redox activity of the cluster of Desulfovibrio gigas ferredoxin II. 1H NMR and Mössbauer spectroscopic study.
Related Articles Thiol/disulfide formation associated with the redox activity of the cluster of Desulfovibrio gigas ferredoxin II. 1H NMR and Mössbauer spectroscopic study.
J Biol Chem. 1994 Mar 18;269(11):8052-8
Authors: Macedo AL, Moura I, Surerus KK, Papaefthymiou V, Liu MY, LeGall J, Münck E, Moura JJ
Desulfovibrio gigas ferredoxin II (FdII) is a small protein (alpha 4 subunit...
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[NMR paper] Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxi
Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin.
Related Articles Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin.
J Biomol NMR. 1994 May;4(3):411-32
Authors: Chandrasekhar K, Campbell AP, Jeng MF, Holmgren A, Dyson HJ
As a prelude to complete structure calculations of both the oxidized and reduced forms of Escherichia coli thioredoxin (M(r) 11,700), we have analyzed the NMR...
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[NMR paper] Thiol/disulfide formation associated with the redox activity of the [Fe3S4] cluster o
Thiol/disulfide formation associated with the redox activity of the cluster of Desulfovibrio gigas ferredoxin II. 1H NMR and Mössbauer spectroscopic study.
Related Articles Thiol/disulfide formation associated with the redox activity of the cluster of Desulfovibrio gigas ferredoxin II. 1H NMR and Mössbauer spectroscopic study.
J Biol Chem. 1994 Mar 18;269(11):8052-8
Authors: Macedo AL, Moura I, Surerus KK, Papaefthymiou V, Liu MY, LeGall J, Münck E, Moura JJ
Desulfovibrio gigas ferredoxin II (FdII) is a small protein (alpha 4 subunit...
Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxi
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