. 2021 Apr 19;6(17):11367–11374. doi: 10.1021/acsomega.1c00343

Table 1. Effect of Helix α1 Mutations on PKR–RNA Binding Affinities^a.

mutant	K_d1 (μM)	K_d2 (μM)	RMSD^b	max RP₂^c
WT	0.166 (0.089, 0.321)	0.487 (0.406, 0.578)	0.0123	0.149
I102A	0.184 (0.104, 0.320)	0.703 (0.593, 0.834)	0.0123	0.112
N106A	0.231 (0.212, 0.252)	0.847 (0.823, 0.871)	0.0076	0.096
R107A	0.225 (0.144, 0.335)	1.103 (0.930, 1.328)	0.0095	0.077
Q110A	0.245 (0.152, 0.376)	1.135 (0.953, 1.379)	0.0103	0.075
K111A	0.399^d	0.564^d	0.0117	0.133

Parameters obtained by global nonlinear least-square analysis of the sedimentation velocity data using a model of sequential binding of two protein monomers. The values in parentheses represent the 95% joint confidence intervals obtained using the F-statistic.

Root-mean-square deviation in absorbance units.

The maximum fractional concentration of the active species containing two PKRs bound to a single RNA at [PKR] = 200 nM.

Confidence intervals could not be obtained.

Table 1. Effect of Helix α1 Mutations on PKR–RNA Binding Affinitiesa.

Table 1. Effect of Helix α1 Mutations on PKR–RNA Binding Affinities^a.