The conserved region is found at the C terminus of most member proteins.

The haem-attachment site is close to the C terminus.

Several alpha-amylases contain a beta-sheet domain, usually at the C terminus.

Additionally, there is a great deal of variability in the C termini, indicating that they might serve subunit specific properties.

There are four conserved predicted alpha helices located towards the C terminus of the protein.

As a protease it cleaves a glycine-glycine dipeptide at its own C terminus.

Its C terminus is membrane anchored.

In eukaryotic Sufu, an additional domain is found at the C terminus of the protein.

It contains a peroxiredoxin-like N-terminus and a glutaredoxin-like C terminus.

The opioid receptor types are 70% identical with differences located at N and C termini.

ELMO1 also has a pro-rich motif at the extreme C terminus.

It is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation.

Each is believed to have 12 transmembrane domains and intracellular N and C termini.

When the passenger domain is translocated, starting with its C terminus, the autochaperone domain is first out.

It is presumed that the active site is located where multiple β-sheet C termini come together in the enzymatic cleft.

This route is expected to take 18 minutes from Arlanda Central to its Uppsala C terminus.

Fpg binds one ion of zinc at the C terminus, which contains four conserved and essential cysteines.

The homeo domain is therefore located closer to the C terminus than in any other known POU protein.

Both the N and M terminals and the C terminus form binding sites to Sup45p, giving a total of two.

The domain is also found in an Olive pollen allergen as well as at the C terminus of family 17 glycosyl hydrolases.

They described a polymorphic site near the C terminus of the coded region, but neither allele at this locus segregated consistently with the atypical trait.

These contain intracellular N and C termini, which form tetramers and vary in length and domain.

The three-dimensional structure consists of a compact disulfide-bonded core from which three loops and the N and C termini emerge.

These results distinguish Ppt1p from mammalian PP5 and suggest that the C terminus is less important in controlling Ppt1p activity.

The motor domain in kinesins is located either in the N terminus, C terminus or in the middle of the protein.

As a result, the C-terminus of the peptide is now ejected.

If this C-terminus is cleaved off, the complex shows greatly reduced attachment ability.

Currently, six different C-terminus splicing variants have been found in normal cells.

Furthermore, different resins allow for different functional groups at the C-terminus.

This domain is found at the C-terminus of several translation Initiation factors.

It is found at the C-terminus of numerous bacterial transcription regulatory proteins.

The C-terminus can also be blocked (thus, neutralizing its negative charge) by amidation.

The C-terminus can contain retention signals for protein sorting.

It can be fused to the C-terminus or the N-terminus of a protein.

It is identical to the C-terminus of myosin light-chain kinase.

It is not clear at present whether phorbol ester effects reflection at the C-terminus.

They are usually represented in protein topology diagrams by an arrow pointing toward the C-terminus.

Both the C-terminus and the N-terminus face the cytoplasmic side of the membrane.

At the C-terminus is the inactive nuclease domain which may function to aid protein stability.

Each subunit possesses a C-terminus and an N-terminus in its sequence.

Other variations associated with H2ABbd are located within its C-terminus.

Proteins are naturally synthesized starting from the N-terminus and ending at the C-terminus.

MH3 is located in the transmembrane forming C-terminus.

It is oriented with the N-terminus outside the cell and the C-terminus in the cytosol.

Secondary structure analysis has predicted that there are alpha-helical regions at both the N and C-terminus.

The chain is linked via its C-terminus to the solid support, with the N-terminus extending off it.

Pom1 phosphorylates Cdr2 on the C-terminus, and prevents it from spreading beyond the medial band.

The C-terminus too is recognized by these furin-like proteases and is also cleaved.

Both the amidated C-terminus and the disulfide bridge are necessary for the full biological activity of amylin.

Sometimes one end of the gene (called the C-terminus) is altered, which interferes with the association of the protein strands.