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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Vydáno v:	Proc Natl Acad Sci U S A
Hlavní autoři:	Gall, C M, Cross, T A, DiVerdi, J A, Opella, S J
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	National Academy of Sciences 1982
Témata:	Research Article
On-line přístup:	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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