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In the overall structure, this complex indicates non-porous structure and the adsorption capabilities toward gaseous organic molecules.
The high value of K value for C60-1 complex indicates that 1 forms an inclusion complex with C60.
The shifts in the Raman peaks from the TCNQ in RGO + TCNQ complex indicates a charge transfer interaction.
The overall conformational change of the complex indicates that TALE repeats may retain structural flexibility even after binding to DNA.
The predicted structure of the Hu 15C1 TLR4 complex indicates that the antibody antagonizes the receptor dimerization necessary for its activation.
Higher magnitude of electronic coupling elements for the C70 1 complex compared to C60 1 complex indicates strong binding between C70 and 1. Steady state fluorescence studies elicit efficient quenching of the fluorescence of 1 in presence of fullerenes.
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spectra were complex indicating that these polymers are essentially atactic.
X-ray powder patterns of the CPC/α-CD complex indicate that the α-CDs units form channels.
In addition, computational predictions of the fitting of saponins to the topoisomerase I DNA complex, indicate a similar binding mode to that of clinically used topoisomerase I inhibitors.
The profiles of TG and DTA curves for [Nd alacac 3]n differ from those for the monomeric complex indicating different mechanisms of thermal decomposition.
Remarkably, this process is also dependent on the PAR-4 kinase complex, indicating the significance of the PAR-4/PIG-1 signaxisg axin in C. elegans.
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