Related ArticlesUse 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 Desulfovibrio vulgaris (Hildenborough) (c3DvH) is determined by means of a novel procedure. In this method the 13C chemical shifts of the nuclei directly bound to the haems are used to determine the in-plane orientations of the rhombic perturbation in each of the four haems with respect to a model of molecular orbitals of e(g) symmetry which are subject to a rhombic perturbation [Turner, D. L., Salgueiro, C. A., Schenkels, P., LeGall, J. & Xavier, A. V. (1995) Biochim. Biophys. Acta 1246, 24-281. These orientations, together with the components of the magnetic susceptibility tensors obtained from the EPR g values and the crystal structure of c3DvH, can be used to calculate the dipolar shifts induced by each haem throughout the protein. Thus the observed 13C paramagnetic shifts of the c3DvH haem substituents were fitted considering both the pseudocontact and contact shifts of each haem simultaneously. The dipolar shifts calculated by this method were tested against the observed dipolar shifts for some amino acid residues strategically placed in the protein and also for the haem propionate groups. The effect of considering the calculated dipolar extrinsic shifts on the behaviour of the chemical shifts of the haem methyl groups in the intermediate stages of oxidation at different pH values was also analysed. The several tests applied to the calculated dipolar shifts have shown that the method is extremely useful for predicting chemical shifts as an aid to complete proton assignment, and to add further constraints in the refinement of solution structures of paramagnetic proteins and hence to probe subtle structural rearrangements around the haem pocket.
Narrowing the conformational space sampled by two-domain proteins with paramagnetic probes in both domains
Narrowing the conformational space sampled by two-domain proteins with paramagnetic probes in both domains
Abstract Calmodulin is a two-domain protein which in solution can adopt a variety of conformations upon reorientation of its domains. The maximum occurrence (MO) of a set of calmodulin conformations that are representative of the overall conformational space possibly sampled by the protein, has been calculated from the paramagnetism-based restraints. These restraints were measured after inclusion of a lanthanide binding tag in the C-terminal domain to supplement the data obtained...
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08-13-2011 02:47 AM
[NMR paper] NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c
NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c552 retains its native structure.
Related Articles NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c552 retains its native structure.
J Biol Chem. 2004 Apr 9;279(15):15177-82
Authors: Wain R, Redfield C, Ferguson SJ, Smith LJ
Conversion of Hydrogenobacter thermophilus cytochrome c(552) into a b-type cytochrome by mutagenesis of both heme-binding cysteines to alanines significantly reduces the stability of the protein...
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11-24-2010 09:25 PM
[NMR paper] 19F NMR of trifluoroacetyl-labeled cysteine mutants of myoglobin: structural probes o
19F NMR of trifluoroacetyl-labeled cysteine mutants of myoglobin: structural probes of nitric oxide bound to the H93G cavity mutant.
Related Articles 19F 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,...
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11-19-2010 08:44 PM
[NMR paper] Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis
Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis.
Biochemistry. 1997 May 27;36(21):6326-35
Authors: Ubbink M, Bendall DS
The complexes of horse ferrous and ferric cytochrome c with Cd-substituted pea plastocyanin have been characterized by nuclear magnetic resonance, in order to determine the binding sites and to study...
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08-22-2010 03:31 PM
[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...
nmrlearner
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08-22-2010 03:31 PM
[NMR paper] Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis
Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis.
Biochemistry. 1997 May 27;36(21):6326-35
Authors: Ubbink M, Bendall DS
The complexes of horse ferrous and ferric cytochrome c with Cd-substituted pea plastocyanin have been characterized by nuclear magnetic resonance, in order to determine the binding sites and to study...
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08-22-2010 03:03 PM
[NMR paper] NMR identification of protein surfaces using paramagnetic probes.
NMR identification of protein surfaces using paramagnetic probes.
Related Articles NMR identification of protein surfaces using paramagnetic probes.
Biochemistry. 1990 Oct 30;29(43):10041-8
Authors: Petros AM, Mueller L, Kopple KD
Paramagnetic agents produce line broadening and thus cancellation of anti phase cross-peak components in two-dimensional correlated nuclear magnetic resonance spectra. The specificity of this effect was examined to determine its utility for identifying surface residues of proteins. Ubiquitin and hen egg white...
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Paramagnetic tagging for protein structure and dynamics analysis
Paramagnetic tagging for protein structure and dynamics analysis
Publication year: 2010
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 12 August 2010</br>
Peter H.J., Keizers , Marcellus, Ubbink</br>
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