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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.