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Rose measured the affinity of Streptococcus mutans to CPP-ACP.
To confirm that the interaction of Rpn13C with Uch37 was specific, we performed surface plasmon resonance (SPR) experiments and measured the affinity between Rpn13C and Uch37.
To determine the energetic importance of conserved nucleotides for SRP assembly, we measured the affinity of the M domain for a series of RNA mutants.
With this aim, we measured the affinity of these peptides on two anti-apoptotic proteins Bcl-xL and Bcl-2 by a polarization fluorescence competitive assay.
We measured the affinity of the H1 subtypes in a band shift assay.
To investigate the reasons of these apparently contradictory data, we measured the affinity of both U2AF65 and SPF45 UHMs and 14-3-3ζ 14-3-3ζ 14-3-3ζtide (Atx1_D_ULM_PE).
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Lastly, in order to quantitatively compare the binding of these mutants to the 60S subunit, we measured the affinities of these mutants to the 60S subunit using Bio-layer interferometry (BLI) (Figs. 3E and S2).
We measured the affinities of VHH-TcTS complexes using a biosensor (Table 2).
The structures of the confirmed hits are shown in Figure 2. In order to further confirm these potential hits, we measured the affinities of the fragments A to E in a radioligand competition binding assay.
Initial matrices are computed by maximizing the centered-kernel alignment (CKA) metric, measuring the affinity between projected samples and labels.
UV-VIS electronic absorption spectra were employed to measure the affinity constants of drug/DNA binding using Scatchard analysis.
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