Below (see Results), we examine binding sites in yeast for several transcription factors, and conclude that dinucleotide correlations are significant in several cases, and occur with gaps of all lengths in a binding region, not just with nearest-neighbours.
We applied this method to examine the binding affinity for a series of published cyclin-dependent kinase 2 (CDK2) inhibitors.
We used fluorescence recovery after photobleaching (FRAP) to characterize the turnover kinetics of impβ at the NPC and to examine the binding affinity of impβ for the pore.
It is worth noting that only a few of the examined binding sites for a given transcription factor have turned out to be functionally important, as in the case of NFκB, AP-1 and SP-1, which have multiple putative binding sites in the TRAIL gene promoter.
To examine relative binding affinities of TRBP-RBD2 for dsRNA, DNA RNA, and dsDNA duplexes, we performed electrophoretic mobility shift assays (EMSA) for solutions containing these duplexes and 0, 1, 3, or 10 μM TRBP-RBD2.
A PerkinElmer Spectrum 100 FTIR-ATR with a diamond crystal was used to examine the fragments for binding medium and pigment identification in the wavenumber range of 400 4000 cm−1 (or 2.5 25 μm).
To address this challenge, we report here, for the first time, the development of the SNPs-seq technology, a high-throughput approach based on massively parallel sequencing strategy to examine SNPs for their protein-binding differences.
The linear camera system used here is ideal for examining binding across flow channels and the deep well depth gives great sensitivity.
To examine the specific binding region for the interaction between SOX4 and KAT5, HEK293 cells were transfected with GFP-fused full-length SOX4 (SOX4 FL) or various SOX4 fragments (F1~F6) together with FLAG-KAT5.
We performed virtual screening (VS) on Zinc database to identify potent dual binding site and selective AChE inhibitors by combining dual pharmacophore models, ADMET screening and finally by docking analysis to examine important interactions responsible for binding to AChE.
