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Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings
Despite their importance for biological activity, slower molecular motions beyond the nanosecond range remain poorly understood. We have assembled an unprecedented set of experimental NMR data, comprising up to 27 residual dipolar couplings per amino acid, to define the nature and amplitude of backb...
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| Main Authors: | , , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
National Academy of Sciences
2005
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1236556/ https://ncbi.nlm.nih.gov/pubmed/16172390 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0505129102 |
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