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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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| Main Authors: | , , , |
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| Format: | Artigo |
| Language: | Inglês |
| Published: |
1982
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| Subjects: | |
| Online Access: | https://ncbi.nlm.nih.gov/pmc/articles/PMC345669/ https://ncbi.nlm.nih.gov/pubmed/6948294 |
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