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. 2014 Apr;20(4):447–461. doi: 10.1261/rna.043034.113

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© 2014 Padlan et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society

This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 3.0 Unported), as described at http://creativecommons.org/licenses/by-nc/3.0/.

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FIGURE 2. — Binding affinities for Lys1 constructs. (A) Binding affinities of full-length aptamer and deletion variants based on footprinting data. (B) Minimization of Lys1 using the predicted secondary structure 1.3 (Lys1.3minA) and secondary structure 1.2 (Lys1.2minB). Residues in gray were changed to CCC to form a thermodynamically stable stem in the Lys1.2minE construct. Residues in bold compose the five Watson-Crick based stems of Lys1.2minF, where UCAGG was replaced with GGGCG and AGUUC was replaced with CCCGC.