. Author manuscript; available in PMC: 2014 Apr 23.

Published in final edited form as: ACS Nano. 2013 Mar 5;7(4):3341–3350. doi: 10.1021/nn400125c

Table 1. The dissociation constant, K_d, of the NCp7 protein-SL3 RNA aptamer complexes.

Values for small and large nanopore data were arrived at using best-fit curves to titrations shown in Fig. 5.

SL3 RNA Aptamer	Small nanopore	Large nanopore	Fluorescence^b
SL3 (GAG)	2 ± 4 nM	278 ± 166 nM	28 ± 2 nM
SL3 (CUG)	1960 ± 300 nM	ND^a	850 ± 250 nM
SL3 (AUA)	ND^a	ND^a	20000 nM

ND stands for not determined data. For large nanopores, we were unable to fit the low-affinity aptamer data to eqn. (3). The binding affinity of the SL3 (AUA) to NCp7, which was obtained from fluorescence measurements, is rounded up to the nearest significant digit.

Fluorescence values are from the literature.³⁶

Table 1. The dissociation constant, Kd, of the NCp7 protein-SL3 RNA aptamer complexes.

Table 1. The dissociation constant, K_d, of the NCp7 protein-SL3 RNA aptamer complexes.