Analysis of the residual alignment of a paramagnetic multiheme cytochrome by NMR
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.
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| Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2014-05, Vol.50 (35), p.4561-4563 |
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| container_end_page | 4563 |
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| container_issue | 35 |
| container_start_page | 4561 |
| container_title | Chemical communications (Cambridge, England) |
| container_volume | 50 |
| creator | Neto, S E Fonseca, B M Maycock, C Louro, R O |
| description | 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. |
| doi_str_mv | 10.1039/c3cc49135h |
| format | Article |
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| fulltext | fulltext |
| identifier | ISSN: 1359-7345 |
| ispartof | Chemical communications (Cambridge, England), 2014-05, Vol.50 (35), p.4561-4563 |
| issn | 1359-7345 1364-548X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1531015062 |
| source | MEDLINE; Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
| subjects | Alignment Couplings Cytochromes Cytochromes c - chemistry Electronic structure Electrons Heme - chemistry Magnetic fields Models, Molecular NMR spectroscopy Nuclear Magnetic Resonance, Biomolecular - methods Orientation Protein Conformation Proteins Shewanella - chemistry Shewanella - enzymology |
| title | Analysis of the residual alignment of a paramagnetic multiheme cytochrome by NMR |
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