Related Articles19F NMR of trifluoroacetyl-labeled cysteine mutants of myoglobin: structural probes of nitric oxide bound to the H93G cavity mutant.
Biochemistry. 2001 Jul 24;40(29):8588-96
Authors: Thomas MR, Boxer SG
Nitric oxide (NO) binds to the myoglobin (Mb) cavity mutant, H93G, forming either a 5- or 6-coordinate Fe--NO heme complex. The H93G mutation replaces the proximal histidine of Mb with glycine, allowing exogenous ligands to occupy the proximal binding site. In the absence of the covalently attached proximal ligand, NO could bind to H93G from the proximal side of the heme rather than the typical diatomic binding pocket on the distal side when the 5-coordinate complex forms. The question of whether NO binds on the distal or proximal side was addressed by (19)F NMR. Site-directed mutagenesis was used to introduce unique cysteine residues at the protein surface on either the distal (S58C) or proximal (L149C) side, approximately equidistant from and perpendicular to the heme plane of both wild-type and H93G Mb. The cysteine thiols were alkylated with 3-bromo-1,1,1-trifluoroacetone to attach a trifluoroacetyl group at the mutation site. (19)F NMR spectra of 5-coordinate, NO bound S58C/H93G and L149C/H93G double mutants depict peaks with line widths of 100 and 23 Hz, respectively. As fluorine peaks broaden with increasing proximity to paramagnetic centers, such as 5-coordinate Fe--NO, the (19)F NMR data are consistent with NO binding in the distal heme pocket of H93G, even in the absence of a sixth axial ligand. Additionally, (19)F NMR spectra are reported for deoxy, oxy, CO, met CN, and met H(2)O forms of the labeled cysteine mutants. These results demonstrate that the fluorine probes are sensitive to subtle conformational changes in the protein structure due to ligation and oxidation state changes of the heme iron in Mb.
Structural characterization of recombinant human myoglobin isoforms by (1)H and (129)Xe NMR and molecular dynamics simulations.
Structural characterization of recombinant human myoglobin isoforms by (1)H and (129)Xe NMR and molecular dynamics simulations.
Structural characterization of recombinant human myoglobin isoforms by (1)H and (129)Xe NMR and molecular dynamics simulations.
Biochim Biophys Acta. 2011 Jul 13;
Authors: Gussoni M, Scorciapino MA, Vezzoli A, Anedda R, Greco F, Ceccarelli M, Casu M
Myoglobin (Mb), the main cytosolic oxygen storage/deliver protein, is also known to interact with different small ligands exerting other fundamental physiological roles. In...
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Expression and purification of (15)N- and (13)C-isotope labeled 40-residue human Alzheimer's ?-amyloid peptide for NMR-based structural analysis.
Expression and purification of (15)N- and (13)C-isotope labeled 40-residue human Alzheimer's ?-amyloid peptide for NMR-based structural analysis.
Expression and purification of (15)N- and (13)C-isotope labeled 40-residue human Alzheimer's ?-amyloid peptide for NMR-based structural analysis.
Protein Expr Purif. 2011 May 27;
Authors: Long F, Cho W, Ishii Y
Amyloid fibrils of Alzheimer's ?-amyloid peptide (A?) are a primary component of amyloid plaques, a hallmark of Alzheimer's disease (AD). Enormous attention has been given to the structural...
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06-07-2011 11:05 AM
[NMR paper] A simple efficient synthesis of [23,24]-(13)C(2)-labeled bile salts as NMR probes of
A simple efficient synthesis of -(13)C(2)-labeled bile salts as NMR probes of protein-ligand interactions.
Related Articles A simple efficient synthesis of -(13)C(2)-labeled bile salts as NMR probes of protein-ligand interactions.
Bioorg Med Chem Lett. 2002 Feb 11;12(3):433-5
Authors: Tochtrop GP, DeKoster GT, Cistola DP, Covey DF
The synthesis of -(13)C(2)-labeled bile salts is achieved through a steroidal side chain degradation and isotopic regeneration strategy. Three common bile acids were degraded to the corresponding C(22 )aldehyde by an...
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[NMR paper] Use of paramagnetic NMR probes for structural analysis in cytochrome c3 from Desulfov
Use of paramagnetic NMR probes for structural analysis in cytochrome c3 from Desulfovibrio vulgaris.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Use of paramagnetic NMR probes for structural analysis in cytochrome c3 from Desulfovibrio vulgaris.
Eur J Biochem. 1997 Mar 15;244(3):721-34
Authors: Salgueiro CA, Turner DL, Xavier AV
The dipolar field generated by each of the four haems in the tetrahaem ferricytochrome c3 from...
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[NMR paper] Use of paramagnetic NMR probes for structural analysis in cytochrome c3 from Desulfov
Use of paramagnetic NMR probes for structural analysis in cytochrome c3 from Desulfovibrio vulgaris.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Use of paramagnetic NMR probes for structural analysis in cytochrome c3 from Desulfovibrio vulgaris.
Eur J Biochem. 1997 Mar 15;244(3):721-34
Authors: Salgueiro CA, Turner DL, Xavier AV
The dipolar field generated by each of the four haems in the tetrahaem ferricytochrome c3 from...
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08-22-2010 03:03 PM
[NMR paper] Identification of cysteine ligands in metalloproteins using optical and NMR spectrosc
Identification of cysteine ligands in metalloproteins using optical and NMR spectroscopy: cadmium-substituted rubredoxin as a model 2- center.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Identification of cysteine ligands in metalloproteins using optical and NMR spectroscopy: cadmium-substituted rubredoxin as a model 2- center.
Protein...
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[NMR paper] Cysteine pairing in the glycoprotein IIbIIIa antagonist kistrin using NMR, chemical a
Cysteine pairing in the glycoprotein IIbIIIa antagonist kistrin using NMR, chemical analysis, and structure calculations.
Related Articles Cysteine pairing in the glycoprotein IIbIIIa antagonist kistrin using NMR, chemical analysis, and structure calculations.
Biochemistry. 1993 Jan 12;32(1):282-9
Authors: Adler M, Carter P, Lazarus RA, Wagner G
The pairing of the cysteines in disulfide bonds was investigated for the 68-residue RGD-containing protein kistrin, a potent antagonist of the integrin GP IIbIIIa and an inhibitor of platelet...
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[NMR paper] NMR study of Galeorhinus japonicus myoglobin. 1H-NMR evidence for a structural altera
NMR study of Galeorhinus japonicus myoglobin. 1H-NMR evidence for a structural alteration on the active site of G. japonicus myoglobin upon azide ion binding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR study of Galeorhinus japonicus myoglobin. 1H-NMR evidence for a structural alteration on the active site of G. japonicus myoglobin upon azide ion binding.
Eur J Biochem. 1991 Jun 1;198(2):285-91
Authors: Yamamoto Y, Chûjô R, Suzuki T...