integral protein

It is an integral protein within the nuclear membrane.

It contains large numbers of integral proteins called porins.

In various other systems, is that an integral protein tends to surround itself by lipids of matching size and shape.

The encoded protein is an integral protein of the plasma membrane containing 12 transmembrane segments.

The interaction of integral proteins with the lipids inside membrane bilayer is of great importance for membrane function.

Facilitated diffusion is the spontaneous passage of molecules or ions across a biological membrane passing through specific transmembrane integral proteins.

Hydrophobic mismatch is the difference between the hydrophobic length of the integral proteins and the hydrophobic thickness of the membrane they span.

Peripheral membrane proteins are temporarily attached either to the lipid bilayer or to integral proteins by a combination of hydrophobic, electrostatic, and other non-covalent interactions.

Emerin, together with MAN1, is a LEM domain-containing integral protein of the inner nuclear membrane in vertebrates.

Polygodial's primary antifungal action is as a nonionic surfactant, disrupting the lipid-protein interface of integral proteins nonspecifically, denaturing their functional conformation.

It contains numerous integral proteins called porins, which contain a relatively large internal channel (about 2-3 nm) that is permeable to all molecules of 5000 daltons or less.

Frizzled is a tissue polarity gene in Drosophila melanogaster and encodes integral proteins that function as cell-surface receptors for Wnts called serpentine receptors.

The channel-forming integral protein, CHIP, is regulated by miR-764-5p at its 3'UTR, and there is negative correlation between expression of the two.

The LEM domain is also common to two other integral proteins of the INM: lamina-associated polypeptide 2 (LAP2) and emerin.

Homology modeling can be used to construct an atomic-resolution model of the "target" integral protein from its amino acid sequence and an experimental three-dimensional structure of a related homologous protein.

APP is a type 1 integral protein that is subjected to a host of post-translational processing events, including N- and O-glycosylation, tyrosyl sulfation, phosphorylation, and proteolysis [39,43,47,48].

The FERM domain allows ERM proteins to interact with integral proteins of the plasma membrane, or scaffolding proteins localized beneath the plasma membrane.

LEM domain-containing protein 3 (LEMD3), also known as MAN1, is an integral protein in the inner nuclear membrane (INM) of the nuclear envelope.

Fibroblast activation protein is a homodimeric integral protein with dipeptidyl peptidase IV (DPPIV)-like fold, featuring an alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain.

Under the consideration of energy requirement, in order to avoid unfavorable exposure of hydrophobic surfaces to a hydrophilic environment, the hydrophobic length of the integral proteins is supposed to be approximately equal to the hydrophobic bilayer thickness.

The glucose transporter of erythrocytes (called GLUT1 to distinguish it from related glucose transporters in other tissues) is a type III integral protein with 12 hydrophobic segments, each of which is believed to form a membrane-spanning helix.

Subsequent investigations showed that rapamycin also binds to this intracellular target, forming an FKBP12-rapamycin complex which is not in itself inhibitory, but does have the capacity to block an integral protein kinase known as target of rapamycin (TOR).

Like the PfMC-2TM proteins, the PfEPF1, 3 and 4 proteins encoded by these families are exported to the Maurer's clefts, as peripheral or integral proteins of the Maurer's cleft membrane and largely exposed to the red cell cytosolic face of this membrane.