Structural and dynamic characterization of the aromatic amino acids of the human immunodeficiency virus type I nucleocapsid protein zinc fingers and their involvement in heterologous tRNA(Phe) binding: a steady-state and time-resolved fluorescence study.

The steady-state and time-resolved fluorescence properties of two zinc-saturated 18-residue synthetic peptides with the amino acid sequence of the NH2-terminal (NCp7 13-30 F16W, where the naturally occurring Phe was replaced by a Trp residue) and the COOH-terminal (NCp7 34-51) zinc finger domains of...

Täydet tiedot

Tallennettuna:
Bibliografiset tiedot
Päätekijät: Mély, Y, Piémont, E, Sorinas-Jimeno, M, de Rocquigny, H, Jullian, N, Morellet, N, Roques, B P, Gérard, D
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: 1993
Aiheet:
Research Article
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC1225878/
https://ncbi.nlm.nih.gov/pubmed/8274645
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