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It has also been predicted to be a 3-pass transmembrane protein.
Thus, it is not predicted to be a transmembrane protein.
It is, however, found to be a transmembrane proteins.
This protein may play a role as a transmembrane protein.
The inactive form is only know to bind to a class of transmembrane proteins.
The last image shows a schematic overview of the transmembrane protein's location.
The sigma-1 receptor is a transmembrane protein expressed in many different tissue types.
This change introduces a further one in the transmembrane protein, opening the pore to at least 6Å.
Thus, a large degree of tilting can be a less favorable option for single transmembrane proteins.
The M2 transmembrane protein is an ion channel required for efficient infection.
This connection may help direct the efforts to elucidate the function of transmembrane protein 131L.
This is the major category of transmembrane proteins.
Ethylene could be perceived by a transmembrane protein dimer complex.
Therefore, transmembrane proteins are corralled by both fences and pickets.
The encoded type 2 transmembrane protein may function as a cell surface antigen.
This putative transmembrane protein is thought to play a role in carbohydrate transport and metabolism.
The protein encoded by this gene is a type I transmembrane protein.
These transmembrane proteins facilitate water passage through the membranes.
These two kinds of specific receptors have some morphological features in common, such as being transmembrane proteins.
Firstly, both of them are usually transmembrane proteins.
More than 40 highly divergent transmembrane proteins that could contribute to this functional diversity have been described.
There are two basic types of transmembrane proteins:
Refolding of α-helical transmembrane proteins in vitro is technically difficult.
Almost all known membrane receptors are transmembrane proteins.
X4 is the protein domain which is a unique type I transmembrane protein.