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Proton-evolved local-field solid-state NMR studies of cytochrome [b.sub.5] embedded in bicelles, revealing both structural and dynamical information
- Source :
- Journal of the American Chemical Society. April 28, 2010, Vol. 132 Issue 16, 5779-5788
- Publication Year :
- 2010
-
Abstract
- Two-dimensional proton-evolved local-field (2D PELF) pulse sequences are implemented by using either composite zero cross-polarization (COMPOZER-CP) or windowless isotropic mixing (WIM) for magnetization transfer. The results from magnetically aligned bicelles containing uniformly [super 15]N-labeled cytochrome [b.sub.5] have shown that the PELF-based experimental approaches have a major impact on solid-state NMR spectroscopy of membrane proteins and other membrane-associated molecules in magnetically aligned bicelles.
- Subjects :
- Cytochromes -- Chemical properties
Cytochromes -- Electric properties
Cytochromes -- Structure
Magnetization -- Analysis
Membrane proteins -- Structure
Membrane proteins -- Chemical properties
Membrane proteins -- Magnetic properties
Nuclear magnetic resonance spectroscopy -- Usage
Chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 00027863
- Volume :
- 132
- Issue :
- 16
- Database :
- Gale General OneFile
- Journal :
- Journal of the American Chemical Society
- Publication Type :
- Academic Journal
- Accession number :
- edsgcl.226419054