Static light scattering may be used to probe the solution behavior of complexes of integral membrane proteins with detergents.
Hydrogen deuterium exchange mass spectrometry (HDX-MS) has become an increasingly routine technology for probing the solution structure and dynamics of proteins.
The results show that the ultra-microelectrodes offer a simple and reliable method of probing the solution composition under conditions where large area electrodes cannot be used.
NMR spectroscopy was therefore used to probe the solution structure of an RNA11 fragment.
Such an initial run enables the modeller to probe the solution space for the existence of multiple minima at low computational cost.
To probe the solution structure and interdomain dynamics of the intact BARD1 C-terminal domain, we next carried out SAXS studies on the intact C-terminal ankyrin-BRCT region of BARD1 (423−777).
The cleaved probes in the solution are then detected with an LF immunoassay.
The mixture was then added to the capture probes, and the solution hybridization was performed for 24 hours at 65 °C.
Samples were rapidly transferred onto ice afterwards, and the empty magnetic streptavidin beads were removed via application of a magnetic field, leaving the washed PRI-lock probes in the solution.
To begin the procedure, a microsyringe slowly pumps the perfusate into the inflow port of the probe, and the solution flows distally through the length of the probe.
