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To date, limited quantitative and behavioral research has been conducted to investigate this interaction or simulate it microscopically.
The objective of the present work was to investigate this interaction process both experimentally and theoretically involving different size of particles (radius ∼ 100 200 μm) with varying surface wettability (contact angle ∼ 50 70°) and a stationary neutrally buoyant immiscible oil-water interface (aniline droplet in salt solution) utilizing high speed imaging technique.
To investigate this interaction we conducted planned comparisons.
We thus set up to investigate this interaction in a direct manner in hippocampal slice preparation.
As the triply phosphorylated peptide did not significantly reduce the binding affinity over the doubly phosphorylated peptide, we did not investigate this interaction further.
To investigate this interaction we conducted planned comparisons, which revealed a rightward bias in the Near within-category and Same category conditions [F (1,9) = 47.9; p<0.0001, F (1,9) = 6.4; p<0.05, respectively].
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We investigated this interaction in model membranes that contain little or no cholesterol with a combination of isothermal titration calorimetry, dynamic light scattering, and zeta potential measurements.
Synthesizing the interaction between all three parameters was difficult because only four studies specifically investigated this interaction.
Paired t-tests comparing within-group mixing costs as a function of CTI variation investigated this interaction.
Considering the recent identification of taperin as a protein mutated in patients with non-syndromic, hereditary deafness, we investigated this interaction in more detail.
Since experiments in two different co-culture systems showed close association of hEPI-NCSC-derived Schwann cells with neurites, we next investigated this interaction at the ultrastructural level in co-cultures of Schwann cells and rat embryo DRG.
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