Specific recognition of the basic N peptide by an RNA

Abstract

Artificial binding model systems with sufficient specificity are indispensable for study and understanding of living systems. Here, we report a small hairpinloop RNA that interacts with a basic peptide derived from bacteriophage lambda N protein, as a new protein-RNA binding model. The RNA was selected in vitro from a hairpinloop RNA library and recognized the target N peptide more specifically than the boxB RNA, the naturally occurring N protein binder.

Thermodynamic Analysis of Duplex Formation of the Heterochiral DNA with l-Deoxyadenosine

“…19 Only the chimeric oligomers with both D-and L-2′-deoxyribose sugars (L/D-DNA) achieved both nuclease resistance and duplex formation, though some decrease of duplex stability was found. [20][21][22] NMR studies for duplexes composed of L/D-DNA and complementary natural DNA (L/D-D duplexes) in which single nucleotide was substituted by L-deoxyguanosine (L-dG) or L-thymidine (L-T) revealed that the structures of the duplexes were normal B-form, and the introduced L-nucleotide formed Watson-Crick hydrogen bonds as normal nucleotides. 23,24 However, these findings do not account for the destabilization of duplexes in the other experiments.…”