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We purified recombinant H1M (Figure 4A), added it to buffer or cytoplasm at a concentration of 1 µM, and measured its binding to chromatin by immunofluorescence of the 6XHistidine tag.

To further characterize HJ16 specificity we measured its binding to two YU2 gp120 mutants: the D368R mutant, which is not bound by CD4 or CD4bs-specific mAbs [21] and the I420R mutant, which is not recognized by CD4i-specific mAbs [62].

Since the [Y]-AII analogue experimentally fulfilled the selectivity criteria for AT2R hypothesized at the onset of this study, we measured its binding to AT1R and AT2R recombinantly expressed in mammalian cells.

We measured its binding affinity for vcCNT using the fluorescence-anisotropy assay and found that the KD decreased by ∼60-fold to 24 μM, suggesting that nucleobase interactions and ribose interactions are additive.

To examine the GTP-loading of Rab11a, we introduced a biotinylated GTP-analog into H9c2-hIR cells, transiently overexpressing HA-tagged Rab11a, and measured its binding to the GTPase after insulin stimulation.

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The correct folding was confirmed by measuring its binding capacity against mAb produced to recognize the native form of MHC molecules by biosensor analysis.

The recognition of gp120 in an oligomeric form by anti-426 MCP MAb (11A8) was examined by measuring its binding to HIV-infected cells using flowcytometry.

To check if this is the case, we thus measured its Ca2+ binding by ITC.

The stratum corneum forms a barrier against diffusion of water through the epidermis; hydration measures its water binding capacity while the measurement of TEWL provides information concerning the integrity of the epidermis.

The activity of the refolded sdAb was determined by measuring its specific antigen-binding ability using indirect ELISA.

MOP dissociation constant was calculated by measuring its competition for NPN binding.

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