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Aromatic Spectral Editing Techniques for Magic-Angle-Spinning Solid-State NMR Spectroscopy of Uniformly (13)C-Labeled Proteins
The four aromatic amino acids in proteins, namely histidine, phenylalanine, tyrosine, and tryptophan, give highly overlapped (13)C chemical shifts between 100 and 160 ppm, and have so far been largely neglected in solid-state NMR determination of protein structures. Yet aromatic residues play import...
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| Veröffentlicht in: | Solid State Nucl Magn Reson |
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| Hauptverfasser: | , , |
| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
2015
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4674322/ https://ncbi.nlm.nih.gov/pubmed/26440131 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.ssnmr.2015.09.006 |
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