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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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Autores principales: Gall, C M, Cross, T A, DiVerdi, J A, Opella, S J
Formato: Artigo
Lenguaje:Inglês
Publicado: 1982
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Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC345669/
https://ncbi.nlm.nih.gov/pubmed/6948294
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