Question 20 If you were and integral membrane protein you would be... Touching exclusively the inner leaflet of the cytoplasmic membrane Floating in the periplasm Embedded in the cytoplasmic membrane Synthetizing integers
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What strategy would you employ to isolate integral membrane proteins vs peripheral membrane proteins? OUTER SURFACE INNER SURFACE (g) GPI anchor (f) Fatty acid or isoprenyl anchor (a) Integral monotopic protein (b) Singlepass protein (c) Multipass protein (d) Multi-subunit protein (e) Peripheral membrane protein Integral membrane proteins Lipid-anchored membrane proteins
Sri K.
Where would you most likely find an integral (transmembrane) protein? on the outside surface of the cell membrane on the inside surface of the cell membrane floating freely in the cytoplasm across the cell membrane
Dominador T.
Correct reference proposed translated polypeptide. It would be an integral membrane protein. It would have 6 transmembrane domains, with the NH2 terminus facing the cytosol and the COOH terminus facing the ER lumen. The NH2 and COOH termini join to form a cytosolic loop. Structurally speaking, the cis network of the Golgi is located in the cis-Golgi network, while the trans network is located in the trans-Golgi network. In the endomembrane system, detergents form micelles instead of bilayers primarily because detergents are non-polar lipids and can only partially dissociate into ions during micelle formation, whereas bilayers are purely lipid membranes and only lipid-protein complexes form. Two types of glycolipids present in the glycocalyx of animal cells are sphingomyelin and cerebrosides. The major role of the protein clathrin during endocytosis is to act as a recognition protein for the binding of SNAREs. Sphingomyelin, glucocerebroside, phosphatidylcholine, and cholesterol cannot undergo flip-flop movement in the membrane. The major difference between the way a protein crosses mitochondrial membranes compared to the way a protein crosses the nuclear envelope is that a protein that crosses the mitochondrial membrane always keeps their signal sequence after they cross, must unfold to be translocated, always crosses one membrane at a time, enters the mitochondrial matrix in the form of membrane vesicles, and finishes their translation once across. High O2 pressure, sodium dodecyl sulfate, pH changes, high salt concentration, and mercaptoethanol can be used to remove integral proteins from their membrane. If a newly synthesized protein had its ER signal sequence at the NH2 terminal and a single stop transfer sequence 1/3 of the way down the length of the polypeptide chain, then we could expect that it would end up as a peripheral protein on the cytosolic face of the ER, not be able to be completely translated by the ribosome, enter the lumen of the ER but would not migrate on to the Golgi, become a transmembrane protein in some structure of the endomembrane system, and have started its translation at the rough ER but the stop sequence would have freed the ribosome from the ER membrane.
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