Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 31, Problem 9P
Interpretation Introduction
Interpretation:
The indicated mechanism needs to be explained.
Concept Introduction:
An integral membrane protein i.e. IMP is a kind of membrane protein which is permanently connected with the biological membrane. All the transmembrane protein are IMPs, but not every IMPs are the transmembrane proteins. IMPs includes a substantial protein’s fraction encoded in the genome of an organism.
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Predict the location(s) (intracellular or extracelular) and a brief description of WHY based on your knowledge of the transport processes in the following constructs. Assume a start codon is present and include any proteolytic processing that would be likely.
1. A PTS1 C-term peroxisomal targeting seq added to C term of a normally secreted protein with usual N -terminal signal sequence
2. Adding of N-terminal mitochondrial targeting sequence to protein with internal nuclear localization seq.
3. Adding N-terminal signal sequence of secreted protein to N-terminus a mitochondria matrix protein precursor with mitochondrial targeting sequence still present
Multipass transmembrane proteins synthesized by ribosomes on the rough endoplasmic reticulum generally have which of the following arrangements of start-transfer and stop-transfer signals?
multiple start signals and multiple stop signals (to allow multiple transmembrane regions)
multiple start signals, but only one stop signal (to allow only one transmembrane region)
only one start signal, but multiple stop signals (to allow only one transmembrane region)
only one start signal, and only one stop signal (to allow only one transmembrane region)
only one stop signal, and only one start signal (to allow only one transmembrane region)
REEP family proteins act as wedges to promote bending of the membrane
true or false
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- Expression of the muscle specific protein dystrophin is important in the functional formation of muscle tissue by integrating the internal cytoskeleton through a transmembrane complex with the extracellular matrix. aiding transcription factors in entry into the muscle cells nucleus degrading non-muscle cell proteins. none of thesearrow_forwardSpecificity in fusion between vesicles involves two discrete and sequential processes. Describe the first of the two processes and its regulation by GTPase switch proteins. What effect on the size of early endosomes might result from overexpression of a mutant form of Rab5 that is stuck in the GTP-bound state?arrow_forwardMaintaining nuclear RanGTP levels is critical for nucleo-cytoplasmic transport. Describe how mutations that disrupt RanGEF function would affect the movement of proteins coming in and going out of the nucleus.arrow_forward
- Describe the structure of SRP in eukaryotes, and outline its role intargeting proteins to the ER membrane.arrow_forwardPlease explainarrow_forwardA. Dr. Randy Schekman introduced you to a yeast model system for studying membrane fusion and vesicle trafficking. Imagine that you have isolated a new temperature-sensitive sec mutant which you suspect has a specific defect in secretory vesicle docking and fusion with the plasma membrane (exocytosis). Describe an experiment you could do to test your hypothesis. B. Now, explain how you would continue your experiment to identify which secretory pathway proteins are present on these secretory vesicles. C. Finally, among the proteins present in these synaptic vesicles according to mass spec you find a protein which contains a G-domain fold suggesting that it is a G-protein. Briefly outline how, in principle, you would determine which of the other proteins is a GAP for this G protein.arrow_forward
- Discuss the three main transport mechanisms for proteins that occur within cells and explain how each mechanism is influenced by cell topology in relation to protein transport among intracellular organelles.arrow_forwardDisulfide bond formation is a regularly observed protien modification that occurs in the lumen of the ER. Explain why disulfifde bond formation is a modification only found in secretory proteins and the extracellular domain of plasma membrane proteins. Furthermore, highlight the advantages disulfide bonds provide to these proteins.arrow_forwardNeed helparrow_forward
- Indicate (x) if the following statements about synthesis of proteins containing an ER signal sequence are True or False: True False i. Translation is initiated by ribosomes located on the ER membrane The signal recognition particle (SRP) binds a sequence of nonpolar (hydrophobic) amino acids. ii. iii. The ER signal sequence may be cleaved by signal peptidase on the cytoplasmic side of the ER membrane. iv. The part of a transmembrane protein that will ultimately be located outside of the cell is inserted into the lumen of the ER during translation. A stop transfer sequence is a series of polar amino acids that halts translocation of a newly synthesized peptide into the ER lumen.arrow_forwardIf membrane proteins are integrated into the ER membrane by means of the ER protein translocator (which is itself composed of membrane proteins), how do the first protein translocation channels become incorporated into the ER membrane?arrow_forwarda. Panels G, H, and I show pattters wher fluorescence is detected in the cytosol or internal cellular membranes. Do these results support the hypothesis that the identity of the beta subunit also plays a role in subcellular localization? b.If co-expression of a given alpha subunit caused the pairs in panels G, H, and I to migrate to the plasma membrane, what would that tell you about the process of plasma membrane localization with heterotrimeric G-proteins containing the beta-5 subunit? (This is all the information that is provided!)arrow_forward
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