Manipulation of the peptide-binding specificity of an RNA in a rational manner by combinations of specificity-altering mutations.

In this study, the potential to manipulate the peptide-binding specificity of an RNA in a rational manner was investigated. First, variants of the Rev-response element (RRE) RNA with different specificities towards the natural binding partner, Rev, and two RRE-binding aptamers, the RSG-1.2 and K1 peptides, were identified.

Tailoring the peptide-binding specificity of an RNA by combinations of specificity-altering mutations.

In this study, the ability to tailor the peptide-binding specificity of an RNA was investigated. First, variants of the Rev-response element (RRE) RNA with different specificities toward the natural binding partner, Rev, and two RRE-binding aptamers, the RSG-1.2 and the Kl peptides, were identified.

Conformational peculiarities of alcohols incorporated in lyotropic and thermotropic liquid crystals.

Conformational characteristics of 1-butanol incorporated not only in hexagonal and lamellar aggregates formed by a lyotropic liquid crystal composed of sodium octanoate, 1-butanol, and water but also in a thermotropic liquid crystal, 4'-methoxybenzylidene-4-n-butylaniline (MBBA), have been investigated from 2H NMR quadrupolar splittings of the perdeuterated and partially deuterated compounds. In the lyotropic phases, 1-butanol shows strong trans preferences and renders itself extended, and octanoate decreases the trans fraction toward the methyl terminal to fill the inner space of the aggregate on behalf of 1-butanol. In MBBA, 1-butanol prefers globular conformations.