In paramagnetic heme proteins, it is often problematic to make the reduced (usually diamagnetic) state lack isotropic shifts proton resonance assignments for heme substituents that do not and are therefore difficult to examine by NMR spectroscopy. have large isotropic shifts and consequently lie und
Recent developments in the13C NMR spectroscopic analysis of paramagnetic hemes and heme proteins
β Scribed by Mario Rivera; GregoriA. Caignan
- Publisher
- Springer
- Year
- 2004
- Tongue
- English
- Weight
- 813 KB
- Volume
- 378
- Category
- Article
- ISSN
- 1618-2650
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13C- and 57Fe-NMR spectra of several carbon monoxide hemoprotein models with varying polar and steric effects of the distal organic superstructure, constraints of the proximal side, and solvent polarity are reported. The 13C shieldings of heme models cover a 4.0 ppm range that is extended to 7.0 ppm
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Analytical biochemistry, in particular the analysis of regulatory proteins that control biological systems and pathways, is dependent on methods of ever-increasing sensitivity. Capillary electrophoresis (CE) has long been recognized as an ultrasensitive analytical technique. In spite of the high sen