Thresholds for extracting DNA/RNA-binding proteins were determined by considering several indices.
The kinetic constants of testosterone- and biotin-binding to steroid-binding proteins were determined with surface plasmon resonance (SPR) analysis.
The abundance of chimeras containing transcription factor among DNA-binding proteins was determined to be (19.5%, P < 6.5E−6).
When the presence or absence of choline-binding proteins was determined for the various strains, substantial strain-to-strain heterogeneity was observed (Technical Appendix 2 Table 2).
Drug binding affinities of mutant proteins were determined, and structures of QacR(E58Q) bound to Be, Dq, and MG and QacR(E57Q) bound to Dq and MG were determined.
The apparent association constants for the binding of radiolabelled RNAs to ZF proteins were determined using a double-filter binding assay.
We assessed mutant C-termini arising from common NMD-R mutations (Table S5) and the top 2% of HLA-A*0201 SYFPEITHI binding scores generated from the mutant proteins were determined (Table 5).
Utilizing the intrinsic fluorescence quenching of tryptophan residues, the binding affinities of wt and mutant QacR proteins were determined for MG and Be.
Similarly, Meis bound at a significantly higher frequency with Pbx than with Foxc1, indicating that the extensive binding overlap of Hox and TALE proteins is determined by other factors in addition to the chromatin structure.
The known inhibitors Lys-Trp-Arg-Arg-Trp-His-Leu, Arg-Trp-His-Arg-Trp-Arg-Leu, Arg-Trp-Arg-Arg-Leu-Thr-Val binding affinity for the target protein were determined by AutoDock as −6.84, −7.21, and −8.52 kcal/mol, respectively.
