Concept explainers
To describe: The two ways in which integral proteins are associated with the plasma membrane.
Introduction: The fluid mosaic model describes the membrane as a phospholipid bilayer in which proteins are embedded to form a mosaic-like pattern. The bilayer ensures the separation of outer content from the content inside the cell. The membrane is semi-fluidic in nature, and the proteins, which are embedded within the membrane, are integral proteins.
To explain: The mechanism of the association of the peripheral proteins with the membrane.
Introduction: The fluid mosaic model describes the membrane as a phospholipid bilayer in which proteins are embedded to form a mosaic-like pattern. The bilayer ensures the separation of outer content from the content inside the cell. The membrane is semi-fluidic in nature, and the proteins, which are embedded within the membrane, are integral proteins.
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Biology
- How long is a typical transmembrane domain, and what is the chemical composition of the amino acids found within the transmembrane domain of a single-spanning integral membrane protein? A~ 20 amino acids; hydrophobic amino acidsB~ 100 amino acids, amphipathic amino acidsC~ 10 amino acids; polar, charged amino acids D~ 50 amino acids, polar, uncharged amino acidsarrow_forwardWhat are the multiple membrane proteins? Describe each of their function.arrow_forwardExplain how the chemical composition/structure of the plasma membrane allows for it to be selectively permeable. What does this information tell you about the chemical composition of an integral protein versus a peripheral protein? How do these differences allow for their different functions?arrow_forward
- What are integral membrane proteins? Under how many types is it examined? Briefly explainarrow_forwardDescribe transmembrane proteins and explain the following roles that they play in the plasma membrane: receptor, enzyme, ion channel, carrier protein, cell-identity marker, and cell-adhesion molecule.arrow_forwardWhat is the structure of the translocation channel that allows transfer of proteins across the membrane bilayer? In particular, is the channel so narrow that proteins can pass through only in an unfolded state, or will it accommodate folded protein domains?arrow_forward
- What would happen in each of the following cases where something related to intracellular transport is altered? Assume in each case that the protein involved is a soluble protein, not a membrane protein. State where each protein would be located and explain each of your answers. You change the hydrophobic amino acids in an ER signal sequence into negatively charged amino acids. You discover a protein that has both an ER signal sequence and a nuclear localization sequence. The ER signal sequence is at the N-terminus of the protein, and the nuclear localization sequence is located in the middle of the protein.arrow_forwardWhy change one type of membrane anchor for another?arrow_forwardWhat is the primary characteristic of peripheral membrane proteins? A: They cannot be post-translationally modified. B: They span the entire lipid bilayer, sometimes multiple times. C: Detergents or nonpolar solvents are necessary to remove them from the lipid bilayer. D:Weak intermolecular forces keep them attached to the lipid membrane.arrow_forward
- A 160 residue polytopic integral plasma membrane protein has the following sequence at its N-terminus. The amino terminal Ser is located inside the cytoplasm. Amino acids 11- 14 are localized outside the cell. N-¹Ser-Tyr-Leu-Gln-Ile-Arg-Phe-Asn-Leu-Lys-11 Gly-Pro-Gly-Ser-15 Glu-Phe-Gln-Leu-Asp- Ile-His-Leu-23 Ser-Gly-Gly Carefully analyze the sequence. (a) What do you predict for the overall tertiary structure of the entire 160 residue protein? (b) Give at least three reasons for your prediction. Ruling out alternatives, with proper logic, can count as a reason.arrow_forwardProteins may be bound to the exoplasmic or cytosolic face of the plasma membrane by way of covalently attached lipids. What are the three types of lipid anchors responsible for tethering proteins to the plasma-membrane bilayer? Which type is used by cell-surface proteins that face the external medium? By glycosylated proteoglycans?arrow_forward1) You are studying a transport protein. It appears to bind temporarily to the molecule to be transported. During normal transport, no energy is expended. The addition of a particular molecule that closely resembles the normally transported molecule inhibits transport. An increase in the concentration of the normally transported molecule in the presence of a constant concentration of the inhibitor increases the rate of transport. What kind of transport is described? 2) What are peripheral membrane proteins?arrow_forward
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