Related ArticlesAnalysis of the residual alignment of a paramagnetic multiheme cytochrome by NMR.
Chem Commun (Camb). 2014 Mar 19;
Authors: Neto SE, Fonseca BM, Maycock C, Louro RO
Abstract
Residual dipolar couplings measured by NMR spectroscopy reveal that the rhombicity of the electronic structure of low-spin paramagnetic hemes determines their relative contribution to the preferential orientation of a protein with multiple hemes when placed in a strong magnetic field.
PMID: 24643435 [PubMed - as supplied by publisher]
[NMR paper] The Structure of the Cytochrome P450cam-Putidaredoxin Complex Determined by Paramagnetic NMR Spectroscopy and Crystallography.
The Structure of the Cytochrome P450cam-Putidaredoxin Complex Determined by Paramagnetic NMR Spectroscopy and Crystallography.
The Structure of the Cytochrome P450cam-Putidaredoxin Complex Determined by Paramagnetic NMR Spectroscopy and Crystallography.
J Mol Biol. 2013 Jul 12;
Authors: Hiruma Y, Hass MA, Kikui Y, Liu WM, Olmez B, Skinner SP, Blok A, Kloosterman A, Koteishi H, Lohr F, Schwalbe H, Nojiri M, Ubbink M
Abstract
Cytochrome P450cam catalyzes the hydroxylation of camphor in a complex process involving two electron transfers from...
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07-17-2013 12:00 PM
Independent alignment of RNA for dynamic studies using residual dipolar couplings
Independent alignment of RNA for dynamic studies using residual dipolar couplings
Abstract Molecular motion and dynamics play an essential role in the biological function of many RNAs. An important source of information on biomolecular motion can be found in residual dipolar couplings which contain dynamics information over the entire ms-ps timescale. However, these methods are not fully applicable to RNA because nucleic acid molecules tend to align in a highly collinear manner in different alignment media. As a consequence, information on dynamics that can be obtained with this method...
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07-20-2012 11:13 PM
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins.
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins.
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins.
J Am Chem Soc. 2011 Feb 2;
Authors: Shi L, Traaseth NJ, Verardi R, Gustavsson M, Gao J, Veglia G
Residual dipolar couplings (RDCs) are widely used as orientation-dependent NMR restraints to improve the resolution of the NMR conformational ensemble of biomacromolecules and define the...
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02-04-2011 11:34 AM
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins
Lei Shi, Nathaniel J. Traaseth, Raffaello Verardi, Martin Gustavsson, Jiali Gao and Gianluigi Veglia
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja109080t/aop/images/medium/ja-2010-09080t_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja109080t
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/Tu9H79dfKCk
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02-03-2011 06:45 AM
[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 03:31 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...
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08-22-2010 03:03 PM
De novo determination of internuclear vector orientations from residual dipolar couplings measured in three independent alignment media
De novo determination of internuclear vector orientations from residual dipolar couplings measured in three independent alignment media
Ke Ruan, Kathryn B. Briggman and Joel R. Tolman
Journal of Biomolecular NMR; 2008; 41(2) pp 61 - 76
Abstract:
The straightforward interpretation of solution state residual dipolar couplings (RDCs) in terms of internuclear vector orientations generally requires prior knowledge of the alignment tensor, which in turn is normally estimated using a structural model. We have developed a protocol which allows the requirement for prior structural knowledge to...
daniel
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08-03-2008 03:54 AM
Composite Alignment Media for the Measurement of Independent Sets of NMR Residual Dipolar Couplings
Composite Alignment Media for the Measurement of Independent Sets of NMR Residual Dipolar Couplings
Ke Ruan and Joel R. Tolman
J. Am. Chem. Soc.; 2005; 127(43) pp 15032 - 15033;
Abstract:
The measurement of independent sets of NMR residual dipolar couplings (RDCs) in multiple alignment media can provide a detailed view of biomolecular structure and dynamics, yet remains experimentally challenging. It is demonstrated here that independent sets of RDCs can be measured for ubiquitin using just a single alignment medium composed of aligned bacteriophage Pf1 particles embedded in a...
Analysis of the residual alignment of a paramagnetic multiheme cytochrome by NMR.
Linear Mode
