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A brief summary of reagents used and the general effects on immune complex binding is shown in Table 1.
The linkage for a model-free binding and a model-dependent binding is shown in Figure 5, where the relationship of macroscopic (stepwise or stoichimetric) binding constants (K1 and K2), overall binding constants (β1 and β2) and microscopic association biding constants, KI and KII is shown.
Physiological relevance of TIRC7 and HLA-DR α2 binding is shown in acute inflammatory setting in vivo after LPS.
The geometry of PA-CD4 with a highest score is shown in Figure 1A, and crystal structure of gp120-CD4 (PDB code 1GC1) binding is shown in Figure 1B.
Residue D161 in TMH 6, thought to be directly involved in substrate binding, is shown in black.
The resistance of trophozoites to the lyses mediated by the r EhCRT-C1q binding is shown in Figure 4.
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The MDs involved in DnaK binding are shown in green, and those that cannot bind to DnaK are shown in red.
Representative titrations for SRC-1 NR2 binding are shown in Figure S3.
The sensorgrams and the kinetic data of the binding are shown in Fig. 3 and Table S4, respectively.
The contacting details of the individual residues involved in binding were shown in Figure 6.
The key residues involved in the pyridine ring binding are shown in red.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com