Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly 13C-labeled proteins
The four aromatic amino acids in proteins, namely histidine, phenylalanine, tyrosine, and tryptophan, have strongly overlapping ¹³C chemical shift ranges between 100 and 160 ppm, and have so far been largely neglected in solid-state NMR determination of protein structures. Yet aromatic residues play...
| Main Authors: | , , |
|---|---|
| Other Authors: | |
| Format: | Article |
| Language: | English |
| Published: |
Elsevier,
2018-01-29T16:15:13Z.
|
| Subjects: | |
| Online Access: | Get fulltext |