In contrast, the interface between the two dimers has few interactions.

This domain only makes a small contribution to the dimer interface.

These additional interactions are expected to enhance the stability of the dimer.

This compound is susceptible to dimer in the gas phase.

This dimer is called a special pair because of its fundamental role in photosynthesis.

Each dimer has about ten thousand atoms in it.

This dimer can be restored by heating to give the monomer.

When lased, the dimer produces light in the ultraviolet range.

The dimer was formed in the gas phase due to the high concentration of the sample.

Zinc metal: Required for coordination between the dimers in the protein.

The dimer is present in a V-shaped form, connected by the hinges.

Breaking the dimer stops the ionic current through the membrane.

Other dimer radical reaction products are formed as well.

This damage is mainly the formation of a thymine dimer.

Classical dimer models have been studied previously in statistical physics.

This domain forms a dimer in the crystal structure.

In solution, this dimer quickly reverts to the blue monomer.

For each mutant we constructed four different kinds of single-chain dimers.

Most dimers in biochemistry are not connected by covalent bonds.

At the protein level, another possibility involves proteins that normally function as dimers.

The vast surface area of the dimer interface indicates that it is biologically significant.

In excess acid conditions the dimer forms the salt.

The enzyme is a dimer, with each subunit containing three domains.

Where represented a covering of a lattice by nearest neighbor dimers.