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Increased Resolution of Aromatic Cross Peaks Using Alternate (13)C Labeling and TROSY
For typical globular proteins, contacts involving aromatic side chains would constitute the largest number of distance constraints that could be used to define the structure of proteins and protein complexes based on NOE contacts. However, the (1)H NMR signals of aromatic side chains are often heavi...
Tallennettuna:
| Julkaisussa: | J Biomol NMR |
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| Päätekijät: | , , , , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
2015
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4782774/ https://ncbi.nlm.nih.gov/pubmed/25957757 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1007/s10858-015-9944-5 |
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