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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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Udgivet i:Proc Natl Acad Sci U S A
Principais autores: Gall, C M, Cross, T A, DiVerdi, J A, Opella, S J
Format: Artigo
Sprog:Inglês
Udgivet: National Academy of Sciences 1982
Fag:
Research Article
Online adgang: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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