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The interplay between transient α-helix formation and side chain rotamer distributions in disordered proteins probed by methyl chemical shifts
The peptide backbones of disordered proteins are routinely characterized by NMR with respect to transient structure and dynamics. Little experimental information is, however, available about the side chain conformations and how structure in the backbone affects the side chains. Methyl chemical shift...
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| Autori principali: | , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Wiley Subscription Services, Inc., A Wiley Company
2011
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3302646/ https://ncbi.nlm.nih.gov/pubmed/21898648 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.726 |
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