These are called peripheral membrane proteins.

The others are called peripheral membrane proteins because they are partially embedded in the bilayer and accomplish the other biological functions.

The nuclear lamin-associated membrane proteins are either integral or peripheral membrane proteins.

Thylakoids contain many integral and peripheral membrane proteins, as well as lumenal proteins.

Peripheral membrane proteins may interact with other proteins or directly with the lipid bilayer.

The regulatory protein subunits of many ion channels and transmembrane receptors, for example, may be defined as peripheral membrane proteins.

Peripheral membrane proteins are proteins that adhere only temporarily to the biological membrane with which they are associated.

Many peripheral membrane proteins bind to the membrane primarily through interactions with integral membrane proteins.

Rab proteins are peripheral membrane proteins, anchored to a membrane via a lipid group covalently linked to an amino acid.

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.

Both Sam35 and Sam37 are located on the cytosolic face of the SAM complex are peripheral membrane proteins that are not essential for survival.

Adrenodoxin and adrenodoxin reductase are soluble peripheral membrane proteins located inside the mitochondrial matrix that appear to associate primarily with each other through electrostatic interactions.

In the case part-way between these two extremes, some peripheral membrane proteins have a patch of hydrophobic amino acids on their surface that locks onto the membrane.

These associate with different peripheral membrane proteins located on the intracellular side of plasma membrane, which anchor the strands to the actin component of the cytoskeleton.

The DPC consists of dystrophin and several integral and peripheral membrane proteins, including dystroglycans, sarcoglycans, syntrophins and dystrobrevin alpha and beta.

Treatment with sodium carbonate (NaCO) detaches peripheral membrane proteins, whereas treatment with detergents and organic solvents solubilizes integral membrane proteins.

In contrast to integral membrane proteins, peripheral membrane proteins tend to collect in the water-soluble component, or fraction, of all the proteins extracted during a protein purification procedure.

Some polypeptide hormones, antimicrobial peptides, and neurotoxins accumulate at the membrane surface prior to locating and interacting with their cell surface receptor targets, which may themselves be peripheral membrane proteins.

The dystrophin-associated glycoprotein (DAG) complex contains various integral and peripheral membrane proteins such as dystroglycans and sarcoglycans, which are thought to be responsible for linking the internal cytoskeletal system of individual myofibers to structural proteins within the extracellular matrix (such as collagen and laminin).

This peripheral membrane protein was implicated as a tumor suppressor.

These are called peripheral membrane proteins.

See also peripheral membrane protein.

An example of a receptor that is a peripheral membrane protein is the elastin receptor.

The others are called peripheral membrane proteins because they are partially embedded in the bilayer and accomplish the other biological functions.

The nuclear lamin-associated membrane proteins are either integral or peripheral membrane proteins.

Thylakoids contain many integral and peripheral membrane proteins, as well as lumenal proteins.

Peripheral membrane proteins may interact with other proteins or directly with the lipid bilayer.

The regulatory protein subunits of many ion channels and transmembrane receptors, for example, may be defined as peripheral membrane proteins.

SCRIB is found in the cell membrane most often as a peripheral membrane protein.

Peripheral membrane proteins are proteins that adhere only temporarily to the biological membrane with which they are associated.

Many peripheral membrane proteins bind to the membrane primarily through interactions with integral membrane proteins.

The cytoplasmic peripheral membrane protein encoded by this gene functions as a protein-tyrosine kinase substrate in microvilli.

The S-Gal protein is a peripheral membrane protein that functions as part of an elastin receptor complex on the surface of cells.

The protein encoded by this gene is a peripheral membrane protein that is a component of tight junctions or TJs.

Rab proteins are peripheral membrane proteins, anchored to a membrane via a lipid group covalently linked to an amino acid.

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.

Both Sam35 and Sam37 are located on the cytosolic face of the SAM complex are peripheral membrane proteins that are not essential for survival.

Adrenodoxin and adrenodoxin reductase are soluble peripheral membrane proteins located inside the mitochondrial matrix that appear to associate primarily with each other through electrostatic interactions.

In the case part-way between these two extremes, some peripheral membrane proteins have a patch of hydrophobic amino acids on their surface that locks onto the membrane.

These associate with different peripheral membrane proteins located on the intracellular side of plasma membrane, which anchor the strands to the actin component of the cytoskeleton.

The site of photosynthesis is the thylakoid membrane, which contains integral and peripheral membrane protein complexes, including the pigments that absorb light energy, which form the photosystems.

SecB maintains preproteins in an unfolded state after translation, and targets these to the peripheral membrane protein ATPase SecA for secretion.

The DPC consists of dystrophin and several integral and peripheral membrane proteins, including dystroglycans, sarcoglycans, syntrophins and dystrobrevin alpha and beta.

Treatment with sodium carbonate (NaCO) detaches peripheral membrane proteins, whereas treatment with detergents and organic solvents solubilizes integral membrane proteins.