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We describe the sample preparation and instrumentation used to visualize the interaction of individual proteins with single molecules of DNA.
The recently developed vector finite element method is used to visualize the interaction of the laser beam with the dielectric object and to quantitatively predict the optical trapping efficiency.
In order to visualize the interaction of endosomes, which contain the internalized viral glycoproteins, with clathrin, actin, dynein and microtubules, a double labeling of viral glycoproteins and different cellular proteins was performed.
The results present new insights into the architecture of tooth-attached biofilms and visualize the interaction of the biofilm with the human immune system.
To visualize the interaction of TNRC6A and Ago2 inside of cell nuclei, we performed immuno-fluorescence microscopy.
With HPF and freeze substitution, it is possible to visualize the interaction of LD with ER membranes without the artifacts that are potentially introduced by chemical fixation, e.g. extraction and/or condensation of proteins and structural distortions.
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To further visualize the interactions of mitochondria and ER, we used structured illumination microscopy (SIM) and found that the colocalization of ER and mitochondria was significantly increased with Hcy treatment for 4 h, from 0.41 ± 0.03 in control T cells to 0.60 ± 0.01 in Hcy-treated T cells (Fig. 5E).
By using ApoTome technology, we can visualize the interactions of endogenous proteins Dnmt1 and PCNA.
Therefore, we visualized the interaction of Mcs1 with F-actin in a microscopic approach using in vitro binding assays and total internal reflection fluorescence microscopy.
The 3-D surface plots of the fitted polynomial regression equations were generated by the software to better visualize the interaction effect of independent variables on responses.
In order to help visualize the interaction network of the oxidative stress across domains we employed Cytoscape 2.6.1.
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