Related Articles13C 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) state. A database of cysteine 13C C(alpha) and C(beta) chemical shifts was constructed from the BMRB and Sheffield databases, and published journals. Statistical analysis indicated that the C(beta) shift is extremely sensitive to the redox state, and can predict the disulfide-bonded state. Further, chemical shifts in both states occupy distinct clusters as a function of secondary structure in the C(alpha)/C(beta) chemical shift map. On the basis of these results, we provide simple ground rules for predicting the redox state of cysteines; these rules could be used effectively in NMR structure determination, predicting new folds, and in protein folding studies.
Rapid, Accurate and Simple Model to Predict NMR Chemical Shifts for Biological Molecu
Rapid, Accurate and Simple Model to Predict NMR Chemical Shifts for Biological Molecules.
Rapid, Accurate and Simple Model to Predict NMR Chemical Shifts for Biological Molecules.
J Phys Chem B. 2010 Nov 18;
Authors: Atieh Z, Aubert-Fre?con M, Allouche AR
We present a new model to predict chemical shifts for biological molecules. It is simple, fast, and involves a limited number of parameters. It is particularly adapted to be used in molecular dynamics studies with a molecular mechanic potential. We test the model for polyamines, which are rather...
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[NMR paper] Unusual 1H NMR chemical shifts support (His) C(epsilon) 1...O==C H-bond: proposal for
Unusual 1H NMR chemical shifts support (His) C(epsilon) 1...O==C H-bond: proposal for reaction-driven ring flip mechanism in serine protease catalysis.
Related Articles Unusual 1H NMR chemical shifts support (His) C(epsilon) 1...O==C H-bond: proposal for reaction-driven ring flip mechanism in serine protease catalysis.
Proc Natl Acad Sci U S A. 2000 Sep 12;97(19):10371-6
Authors: Ash EL, Sudmeier JL, Day RM, Vincent M, Torchilin EV, Haddad KC, Bradshaw EM, Sanford DG, Bachovchin WW
13C-selective NMR, combined with inhibitor perturbation...
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11-19-2010 08:29 PM
[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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08-22-2010 03:33 AM
[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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08-22-2010 03:33 AM
[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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Journal club
0
08-22-2010 03:33 AM
[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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08-22-2010 03:33 AM
[NMR paper] Engineering out motion: a surface disulfide bond alters the mobility of tryptophan 22
Engineering out motion: a surface disulfide bond alters the mobility of tryptophan 22 in cytochrome b5 as probed by time-resolved fluorescence and 1H NMR experiments.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Engineering out motion: a surface disulfide bond alters the mobility of tryptophan 22 in cytochrome b5 as probed by time-resolved fluorescence and 1H NMR experiments.
Biochemistry. 1999 Apr 20;38(16):5065-75
Authors: Storch EM, Grinstead JS, Campbell AP, Daggett V, Atkins WM
...
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08-21-2010 04:03 PM
Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts
Abstract We present a program, named Promega, to predict the Xaa-Pro peptide bond conformation on the basis of backbone chemical shifts and the amino acid sequence. Using a chemical shift database of proteins of known structure together with the PDB-extracted amino acid preference of cis Xaa-Pro peptide bonds, a cis/trans probability score is calculated from the backbone and 13Cβ chemical shifts of the proline and its neighboring residues. For an arbitrary number of input chemical shifts, which may include Pro-13Cγ, Promega calculates the statistical probability that a Xaa-Pro peptide bond...
13C NMR chemical shifts can predict disulfide bond formation.
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