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Probability-based protein secondary structure identification using combined NMR chemical-shift data
For a long time, NMR chemical shifts have been used to identify protein secondary structures. Currently, this is accomplished through comparing the observed (1)H(α), (13)C(α), (13)C(β), or (13)C` chemical shifts with the random coil values. Here, we present a new protocol, which is based on the join...
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| Autori principali: | , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Cold Spring Harbor Laboratory Press
2002
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2373532/ https://ncbi.nlm.nih.gov/pubmed/11910028 |
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