Assignment of the 13C and 13CO resonances for Rhodobacter capsulatus ferrocytochrome c2 using double-resonance and triple-resonance NMR spectroscopy
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1994.tb18715.x/fullpdf
Reference77 articles.
1. 13C nuclear magnetic resonance spectra of coproporphyrins
2. Cytochromec2- an electron carrier shared by the respiratory and photosynthetic electron transport chain ofRhodopseudomonas capsulata
3. 1H1H correlation via isotropic mixing of 13C magnetization, a new three-dimensional approach for assigning 1H and 13C spectra of 13C-enriched proteins
4. Optimized recording of heteronuclear multidimensional NMR spectra using pulsed field gradients
5. Molecular structure of cytochrome c2 isolated from Rhodobacter capsulatus determined at 2·5 Å resolution
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1. Main Chain and Side Chain Dynamics of a Heme Protein: 15N and 2H NMR Relaxation Studies of R. capsulatus Ferrocytochrome c2;Biochemistry;2001-05-09
2. Magnetic Susceptibility Tensor and Heme Contact Shifts Determinations in the Rhodobacter capsulatus Ferricytochrome c‘: NMR and Magnetic Susceptibility Studies;Journal of the American Chemical Society;2001-02-15
3. Solution structure of the functional domain ofParacoccus denitrificanscytochromec552in the reduced state;European Journal of Biochemistry;2000-07
4. Sequence-specific NMR assignment of proteins by global fragment mapping with the program MAPPER;Journal of Biomolecular NMR;2000
5. Redox‐related conformational changes inRhodobacter capsulatuscytochromec2;Protein Science;2000-01
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