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Serum Preclinical CartiLaps ELISA is based on the binding of two identical monoclonal antibodies to cross-linked serum fragments of type II collagen.
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Ligand binding induces dimerization of two identical (homodimer) or different (heterodimer) receptors.
As BH4-containing and -deficient nNOS were expected to have the radioligand bound at the low- and the high-affinity site respectively, this observation argued strongly in favor of two identical anticooperative binding sites.
Sulfate ABC transporters in cyanobacteria and proteobacteria consist of two identical ATP-binding CysA proteins, two transmembrane proteins (CysT and CysW), and a sulfate-binding protein SbpA.
Kinesin-1 is a dimer that consists of two identical motor domains (heads), which both contain an ATP-binding pocket and a microtubule-binding domain (Vale and Milligan, 2000).
This 1 MDa hetero-oligomer consists of two identical stacked rings assembled from eight paralogous subunits, each containing a conserved ATP-binding domain.
This 1 MDa hetero-oligomer consists of two identical stacked rings assembled from eight paralogous subunits, each containing a conserved ATP-binding domain.
It is composed of two identical windings.
Only one involved the purchase of two identical knives.
We note in this scenario, two ISRIB molecules binding to two identical interfaces of opposite polarity (eIF2B2 → eIF2B4 and eIF2B4 → eIF2B2) may bind and stabilize one (eIF2B 2, which may contribute to its potency.
Each streptavidin molecule is a tetramer of four identical biotin binding subunits, and the entire tetramer is roughly ellipsoidal with axes of 5.4 nm × 5.8 nm × 4.8 nm.
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