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Protein dynamics by solid-state NMR: aromatic rings of the coat protein in fd bacteriophage.
The motions of the aromatic amino acids of the fd bacteriophage coat protein are described by solid-state 2H, 13C, and 15N NMR. Tryptophan-26 is immobile on time scales as slow as 10(3) HZ. The phenylalanine and tyrosine rings undergo 180 degree flips about the C beta--C gamma bond axis more often t...
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| Publicado en: | Proc Natl Acad Sci U S A |
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| Autores principales: | , , , |
| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
National Academy of Sciences
1982
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC345669/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6948294/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.79.1.101 |
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