RNA binding analysis indicated that the single-nucleotide change reduced the ability of 3′UAR-PPMO to block the RNA/RNA interaction required for genome cyclization.
Importantly, the results of this binding analysis indicated that maximum zipper heterodimer formation occurs with the corresponding zipper-scFv when the R-R34 and EE12RR345L zipper domains are located on the C-terminus of either the 566FF fiber or the fiber-fibritin knob deleted fibers (Table 1).
On the other hand, structural analysis indicates that GA binding results in an increased hydrophobicity around the tryptophan residues of BSA as revealed by the synchronous fluorescence spectra, and a decrease in α-helix as revealed by the far-UV CD spectra.
This analysis indicates that, upon binding to SC18 and to a lesser extent NY18, LSTc undergoes a conformational change, reducing the θ angle and subsequently the level of conformational freedom of the Neu5Ac residue, particularly in the region between atoms C6 and C9.
The above analysis indicates that the bindings of Lats1/2-FBD and Merlin-CTD to the FERM domain are mutually exclusive, and thus the auto-inhibited conformation of Merlin is expected to prevent Lats1/2 from binding to Merlin.
Our analysis indicates that structures of binding sites and their fluctuations (Fig. 3) are associated with the global minimum of the PMF.
The promoter of the luxR gene of V. fischeri, for instance, has been shown to bind LexA and its own product (LuxR), which share the same binding site [ 70, 71], and our analysis indicates that this cross-regulation is maintained in the closely related A. salmonicida.
Our GO analysis indicates that signaling and binding processes are important biological activities associated with phloem cells.
The analysis indicates that some interesting binding motifs can be found, such as neural-specific Elavl2, cytokine's degrading Zfp36, and mRNA trafficking Khsrp.
Electrostatic potential analysis indicates that the antigen-binding site of R53 is negatively charged, complementing the positively charged epitope that harbors two positively charged residues, LysP432 and ArgP440.
