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In order to determine whether the calcium effect on MEKK2-Lad1 isteraction is direct or mediated by other interacting proteins, we further examined the interaction by an in vitro binding assay.
These findings were further supported by detailed measurements of the thermochemistry of the interaction by ITC.
We confirmed the interaction by an in vitro pull-down assay with recombinant proteins of GST-ULK1 279–525 and His-STX17 157–275.
First, a novel protocol that structures the interaction by capturing the commitments that agents incur when using rewards.
Whilst we have not been able to model the interaction of HAdV-D26 or D48 with DSG2, due to the lack of an available high-resolution complexed structure at the time of writing, we investigated the interaction by SPR analysis.
The modulation of the interaction by calcium ions makes it unique among the currently known binding mechanisms of proteinaceous α-amylase inhibitors.
It is shown that with simple modifications, the Interaction by Exchange with the Mean mixing model is able to predict the flame quite accurately.
To model the small-scale mixing of the transported scalar, the interaction by exchange with the conditional mean (IECM) model is adopted.
The functional form of the conditionally filtered diffusion is well described by the Interaction by Exchange with the Mean (IEM) model.
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Here, the reaction is studied in conjunction with the interaction-by-exchange-with-the mean (IEM) model of micromixing.
The mesomixing and the micromixing contributions in the PDF equation are closed using the gradient-diffusion model and the Interaction-by-Exchange-with-the-Mean (IEM) model, respectively.
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