The monomeric form adopts a bent structure very similar to that of sulfur dioxide with a bond length of 161 pm.

It is believed that the two separate catalytic sites fused into a single protein to stabilize its monomeric form.

As a homodimer it is still able to bind to muscle type and α7 nAChRs, but with a lower affinity than in its monomeric form.

It has been proposed that p66 in a monomeric form exists in a closed conformation similar to p51 [ 26 ] .

The four PDGFs are inactive in their monomeric forms.

It has been modified to generate a monomeric form (referred to as mEos) that is more amenable for experiments involving labeling of a single molecule.

Because Eos is available in monomeric forms, it can also be used to observe the kinetics and trafficking of single molecules as a fusion protein.

Most recently, the monomeric form seems to be favored by most researchers.

The linear shape of the monomeric form is as predicted by VSEPR theory.

It is this monomeric form that displays the typical staggered metallocene sandwich structure.