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- W2057201654 abstract "The ability of RNA structures to adopt diverse yet complex tertiary structures has resulted in numerous fascinating RNA-protein recognition events. It was recently reported that a close relative of the HIV Rev peptide, namely a 17 residue Tat peptide from bovine immuno-deficiency virus (BIV), is able to bind to the 28 nucleotide BIV TAR RNA construct. Here we report that by simply converting the 17 residue β-ribbon peptide structure to a 19 residue cyclopeptide, the binding affinity (Kd) of the resulting cyclopeptide to the TAR RNA target, observed by fluorescence binding study, was enhanced approximately 5-fold." @default.
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- W2057201654 date "2001-01-01" @default.
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- W2057201654 title "Binding of a cyclic BIV β-tat peptide with its TAR RNA construct" @default.
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- W2057201654 doi "https://doi.org/10.1016/s0960-894x(00)00591-6" @default.
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