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/content/avs/journal/bip/3/2/10.1116/1.2921867
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48The reference patches BSA and dextran show nonspecific adsorption of histidine-tagged receptors. This adsorption seems to be of a highly unstable nature as it bleeds completely off the surface with time. A related observation from the experiment is that when the vesicles were loaded with a relatively high concentration of receptor proteins, a certain loading level was passed, after which an unstable immobilization can be seen dissociation. However, the dissociation levels off at a value at which it is stable. When lower amounts of proteins were injected, below that value, the immobilization was observed to be stable from the start data not shown. We believe this to be the result of an interaction between the histidine-tagged and loosely associated ions (Ni2+) on the surface (i.e., the BSA, dextran, and c-DNA tags of the vesicles.
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49The B′ and D′ systems show a higher degree of repeatability in the signals compared to the A′ and C′ systems, which display a higher internal variance. This variation is an effect of the dispensing protocol; as the dispensing was manual and the location of the dispensing spots had to be revealed, water was evaporated on the array. Ideally, dispensing should occur as soon as the pattern is visible, but, in many cases, it got delayed and the formation of larger condensation droplets of water occurred before the spot was covered with the dispensing NA-ssDNA solution. Diffusion of proteins into the water droplets is relatively slow, which means that these areas of the spots will only partially be modified by NA-ssDNA and cannot fully interact with the vesicles. However, the variation remains consistent proportional throughout the whole time and is easily resolved by scaling as is shown ahead.
50.
50{au{gnG. L.} {fnZubay}}, {btBiochemistry}, {en4th} ed. {ei{fnBrown}}, {ei{fnDubuque}, {gnIA}}, ({dy1998}).
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