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In order to understand the contributions of individual amino acid residues to this complex binding mode, N-terminal deletions and point mutations have been introduced, and the binding properties of each mutant inhibitor protein have been examined.
In this study, the intrinsic calcium binding properties of each C2 domain were measured using isothermal titration calorimetry (ITC).
The binding properties of each of the IFNα and IFNβ proteins for IFNAR1 can vary, depending on interaction of the cytokine with defined amino acids of the receptor [ 32].
While subtle differences in the binding properties of each of the interferons to IFNAR, their common receptor, have been predicted based on analysis of their amino acid sequence and mutation studies, and there are demonstrated differences in engaging downstream signaling components by the two type I interferon subtypes, their functional impact on gene expression is quite comparable [ 32- 34].
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The metal-binding properties of each mutant were examined by DSC.
The carbohydrate-binding properties of each lectin were responsible for the different binding patterns observed.
To compare the binding properties of VEGF121, VEGF165 and VEGF189, we fused each isoform to AP and performed in situ ligand binding assays on E12.5 hindbrains.
Saturation binding studies were carried out to analyse the in vitro binding properties of the diabody.
Binding properties of 68Ga-THP-mal-J591c-scFv were analysed in homologous competition studies [17].
The binding properties of isomiRs to their mRNA targets may vary (Baccarini et al., 2011).
Binding properties of the radiolabelled diabody were analysed in homologous competition studies.
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