Very little is known about the structure of this fundamental protein complex.

Four large protein complexes take part in the light stage.

Many other proteins assemble with Dcp2 to form a protein complex.

A protein complex that contains two or more different polypeptides.

That meant there would be more than one gene coding for the large protein complex.

It can also refer to a protein complex made of two or more subunits.

These segments are essential for the assembly of certain protein complexes.

Separate and purify the individual chains of the protein complex, if there are more than one.

The tool can identify the dynamic protein complex regulation under different condition or time points.

The radial spoke is another protein complex of the axoneme.

Mathematically, a matrix model of a protein complex is a complete graph.

This model also explains how large protein complexes might form at the nuclear envelope (see below).

Protein binding to form a protein complex is also another possibility.

This was also significant, since it was the first structure for any membrane protein complex.

It is associated with the multimeric polycomb group protein complex.

This change increased the affinity of the protein complex for 2,6-dichlorophenol-indophenol at its oxidation sites.

"Now we are accurately determining the crystal structure of the protein complex.

Alternative splicing takes place in a large protein complex called the spliceosome.

A light chain is the small polypeptide subunit of a protein complex.

On the other hand, the ability for these methods to make a prediction is constrained by a limited number of known protein complex structures.

Neuroproteomics is the study of the protein complexes and species that make up the nervous system.

One possibility is that as a protein complex it binds to the chromatin.

The team has also come up with a second design of the protein complex the photosystem II.

The immobilized protein complex can be accomplished either in a single step or successively.

This time she looked closely at the transcription factors that triggered expression of the large protein complex.

A common feature appears to be involvement in multiprotein complexes.

The structure of proteins play a role in how the multiprotein complex assembles.

Hsp90 acts in a multiprotein complex with several co-chaperones.

The cohesin multiprotein complex is required for sister chromatid cohesion.

The term "monomeric protein" may also be used to describe one of the proteins making up a multiprotein complex.

Their interaction results in formation of multiprotein complexes.

Mediator is a multiprotein complex that functions as a transcriptional coactivator.

Proper assembly of multiprotein complexes is important, since misassembly can lead to disastrous consequences.

Other assemblies referred to instead as multiprotein complexes also possess quaternary structure.

It has, therefore, been proposed that the J domain is involved in the rearrangement of multiprotein complexes.

CsoS3 may not interact, or it may only bind, in fully formed multiprotein complexes.

The recruitment of PP2A has been shown to be mediated by the multiprotein complex.

In yeast and rat, Sec15 is part of a multiprotein complex that is required for targeted exocytosis.

Both lead to the release of CAR from the multiprotein complex and its translocation into the nucleus.

These stable interactions involve cell junctions which are multiprotein complexes that provide contact between neighboring cells.

A multiprotein complex (or protein complex) is a group of two or more associated polypeptide chains.

Due to its multiple interactions, VirB8 is an excellent model for the analysis of assembly factors of multiprotein complexes.

PcG proteins function as multiprotein complexes.

It seems to interact in a multiprotein complex with RbAp48 and HDAC3.

Elaborate multiprotein complexes function in allowing access of regulatory proteins to the DNA template.

While the ribosome is the most commonly observed intracellular multiprotein complex in bacteria other large complexes do occur and can sometimes be seen using microscopy.

More recently, it was discovered that certain multiprotein complexes containing succinate dehydrogenase can provide activity similar to that of K channels.

The cell uses limited proteolytic activity at sites of individual focal adhesions via the formation of multiprotein complexes.

The dystrophin-associated protein complex is a multiprotein complex that includes dystrophin and the dystrophin-associated proteins.

Nascent peptides reach the ER via the Translocon, a membrane-embedded multiprotein complex.