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- 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.175. A 70-year-old man comes to the physician because of a 1-month history of heavy, pressing substernal chest pain that occurs when he walks up a flight of stairs. The symptoms are relieved by rest. The physician prescribes a drug to alleviate the symptoms. Within the cell, the drug acts by breaking down into a compound that binds to a protein to increase intracellular concentrations of cGMP, resulting in vasodilation. This binding most likely occurs in which of the following cell locations? A) Cytosol B) Golgi complex C) Mitochondria D) Nucleus E) Peroxisome F) Plasma membrane98.Describe the mechanism for fast ligand-gated channels and the types of changes they can produce in the cell membrane.
- 94. What are the types of non-covalent bonds between the amino acid side chain with the receptor?The peptide Leu-Cys-Arg-Ser-Gln-Met is subjected to Edman degradation. After the first cycle of this process, the products that are generated are: O PTH-Leu, PTH Cys, PTH-Arg. PTH-Ser, PTH-GIn, and PTH-Met O PTH-Leu-Cys-Arg-Ser-Gin-Met O PTH-Met and Leu-Cys-Arg-Ser-Gin-Met O PTH-Leu-Cys and PTH-Arg-Ser-Gin-Met O PTH-Leu and Cys-Arg-Ser-Gln-MetOther than the substitution of uracil for thymine, how doRNA nucleotides differ from DNA nucleotides? (Hint: Reviewsection 2.4.)
- 6) Proteins can be modified by phosphorylation, which adds a phosphate group to the hydroxyl group of serine, threonine, or tyrosine residues. The R-group for phosphoserine is shown at right. A) The image below is an Isoelectric focusing strip that shows the unphosphorylated protein-of-interest (in blue). To which side of the unphosphorylated protein would you expect to see the phosphorylated protein? (Draw an arrow to indicate direction). Briefly justify your answer. un-phosphorylatable: Low pH Justify: B) To study the effects of phosphorylation, researchers often mutate a Ser/Thr to appear as though it is always phosphorylated or never phosphorylated at a particular site. What amino acid substitution should you use to preserve similar dimensions as Ser (or Thr) but make the side chain appear to be: constitutively (always) phosphorylated: Justify: Ser or Thr → O O=P-O O I CH₂ Ser or Thr➜ Phosphoserine High pHIn the protein adenylate kinase, the C-terminal region has the sequence Val-Asp-Asp-Val-Phe-Ser-Gln-Val-Cys-Thr-His- Leu-Asp-Thr-Leu-Lys- The hydrophobic residues in this sequence are presented in boldface type. Suggest a possible reason for the periodicity in their spacing.In the protein adenylate kinase, the C-terminal region has the sequence Val-Asp-Asp-Val-Phe-Ser-Gln-Val-Cys-Thr-His-Leu-Asp-Thr-Leu-Lys-The hydrophobic residues in this sequence are presented in boldface type.Suggest a possible reason for the periodicity in their spacing.
- . In the protein adenylate kinase, the C-terminal region is a-helical, with the sequence Val-Asp-Asp-Val-Phe-Ser-Gin-Val-Cys-Thr-His-Leu-Asp- Thr-Leu-Lys- The hydrophobic residues in this sequence are presented in boldface type. Suggest a possible reason for the periodicity in their spacing.How are H^3 peptides used to study intracellular pathways?For each of the following, describe the path the protein takes to its final destination in the cell.Drawings are strongly recommended! If you need more space, you can use a separate sheet ofpaper. Proteins: 1) Hedgehog (released from the signaling cell), 2) Smoothened, 3) Ci/GliYour answers should include the following if they apply for each protein:o Sorting sequences and how the protein knows where to go at each step (what recognizesdifferent sorting sequences/tags). How/when the protein is inserted into the membrane (if it is a membrane protein) What organelles the protein passes through on its way to its final destination. How the protein is transported (vesicles? translocons? etc.), including a role for microtubules.How the protein might be modified in each organelle it passes through. What other proteins are involved in transport and how the system is reset to allow for otherproteins to be transported.