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Arsenic binding studies were undertaken under conditions optimized with respect to the crucial separation factor of the nonapeptides vasotocin (Vtc) and vasopressin (Vpr) in a shortened gradient time of 7.5 min.
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Molecular-docking, molecular dynamics (MD) simulation and fluorescence-binding studies were undertaken to understand the role of N-terminal 59-residues in the binding of substrate/inhibitors. Molecular docking studies revealed that the PKR-inhibitor binds in the large hydrophobic cavity of the kinase domain of MARK4 through several hydrophobic and hydrogen-bonded interactions.
Therefore, a systematic binding study was undertaken to assess the preferences of FXR1 and FXR2 for the varying methylation states at these lysine sites.
Given that the intracellular domain of IL-13Rα2 only contains a 17-amino-acid structure that lacks protein binding motifs, studies were undertaken to define the role of this domain in Chi3l1/YKL-30/BRP-39 signaling events.
FACS and BIAcore binding specificity and affinity studies were undertaken as described previously (Liu et al, 2003).
With the aim to elucidate the structural features governing the differential inhibitory binding behavior of these inhibitors, molecular modeling studies were undertaken to generate atomic models compatible with the experimental data available.
Methods: Two separate studies were undertaken.
In 2010, two such studies were undertaken.
Both experimental and numerical studies were undertaken.
Bench scale laboratory studies were undertaken.
Three distinct studies were undertaken sequentially.
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