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In vitro binding studies show that F-SRC-1 binds to a variety of nuclear hormone receptors in a ligand-dependent manner, along with TBP and TFIIB, suggesting that F-SRC-1 may play a role as a bridging molecule between nuclear hormone receptors and general transcription factors.
The binding studies show that the CTD of primase binds with a high affinity to the full length helicase and NTDL; poorly with NTD of HpDnaB alone.
Competition binding studies show that ADP and AMP-P-N-P bind with a 5- and 55-fold lower affinity, respectively, than ATP.
Crystallographic and solution binding studies show that E. coli Hfq has preferences to bind an A-A-N motif on the distal face (Robinson et al., 2013 ).
Peptide binding studies show that the overlapped PAM2 motifs of eRF3 binding with significantly (up to 30 fold) higher affinity than the PAM2 motifs of PAN3 and Tob [12], [28], [32].
These binding studies show that attachment of C3b molecules to a surface alters the binding affinity of C5 for C3b.
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In vitro binding studies showed that Pho4 binds cooperatively with Pho2 at UASp1 [31].
NMR titration experiments mapped the binding surface of the hSRI domain to helices 1 and 2, and Biacore binding studies showed that the domain binds preferably to [Ser-2 + Ser-5]-phosphorylated CTD peptides containing two or more heptad repeats.
Furthermore, binding studies showed that oxysterols did not compete with fluorescently labeled cyclopamine, BODIPY-cyclopamine, for direct binding to Smoothened.
Optical biosensor binding studies showed that the one of the CV-N-binding peptide, TN10-1, bound to CV-N with a KD value of 1.9 μM.
The in vitro binding studies showed that the mechanism of anticonvulsant activity may be partially related with the influence on the voltage-gated sodium and calcium channels.
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