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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...
Gorde:
| Egile Nagusiak: | , , , |
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| Formatua: | Artigo |
| Hizkuntza: | Inglês |
| Argitaratua: |
1982
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| Gaiak: | |
| Sarrera elektronikoa: | https://ncbi.nlm.nih.gov/pmc/articles/PMC345669/ https://ncbi.nlm.nih.gov/pubmed/6948294 |
| Etiketak: |
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