How many moles of ATP and GTP are required to synthesize a mole of a polypeptide 100 amino acids long? Hint: remember you need nucleotide triphosphates for both charging the tRNAS and for direct synthesis of polypeptide chains by the ribosome.
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- Imagine you need to move a large protein from one region in the cell to another. Which of the following proteins would be able to do this? Onuclease O myoglobin O kinesin Oligase O hemoglobin O myosinWhat is the smallest number of molecules of ATP and GTP consumed in the synthesis of a protein with 200 residues after mRNA synthesis, starting from amino acids? Assume that the hydrolysis of PP; is equivalent to the hydrolysis of ATP for this calculation. number of ATP molecules: number of GTP molecules: 400 800 IncorrectAllosteric Regulation of Ribonucleotide Reductase by ATP and Deoxynucleotides Describe the underlying rationale for the regulatory effects exerted on ribonucleotide reductase by ATP, dATP, dTTP, and dGTP.
- You are studying an E. coli gene that specifies a protein. A part of its sequence is–Ala–Pro–Trp–Ser–Glu–Lys–Cys–His–You recover a series of mutants for this gene that show no enzymatic activity. By isolating the mutant enzyme products, you find the following sequences:Mutant 1:–Ala–Pro–Trp–Arg–Glu–Lys–Cys–His–Mutant 2:–Ala–Pro–Mutant 3:–Ala–Pro–Gly–Val–Lys–Asn–Cys–His–Mutant 4:–Ala–Pro–Trp–Phe–Phe–Thr–Cys–His–What is the molecular basis for each mutation? What is the DNA sequence that specifies this part of the protein?Many enzymes are switched "on" by attachment of a phosphate group at a specific serine somewhere on the protein (phosphorylation). The basic reaction is: E + ATP2 Ep + ADP Po SERINE PHOSPHO SERINC (Note the "squiggles" before the backone amide and carbonyl indicate the polypeptide chain continues on either side of the serine). For phosphorylation to have this effect, there has to be some equilibrium between inactive and active forms conformations of the enzyme: [Eactive] [Einactive] Einactive 2 Eactive; K* The same basic equilibrium must exist for the phosphorylated protein: [Ep,active] [Ep,inactive] EP,inactive 2 Ep,active; Kp = (a) If phosphorylation increases the measured activity of the enzyme, is K* or K larger? Why? (b) Does the phosphorylation site need to be near the site where the enzyme binds its substrate (e.g. the reactant whose chemistry it catalyzes)? Why or why not?Chart is Given for you: Below is a chart of values for actual enzymes. Enzyme Km (M) kcat (1/s)Chymotrypsin 1.5 × 10^−2 0.14Pepsin 3.0 × 10^−4 0.5Tyrosyl-tRNA synthetase 9.0 × 10^−4 7.6Ribonuclease 7.9 × 10^−3 7.9 × 10^2Carbonic anhydrase 2.6 × 10^−2 4.0 × 10^5Fumarase 5.0 × 10^−6 8.0 × 10^2 Assume the enzyme concentration is equal across all samples (and is equal to 1). (Answer a and b only)a. Which enzyme will have the highest V0 at very high substrate concentrations? (1 M). Why? b. Which will have the highest V0 at very low substrate concentrations (5.0 × 10^−12). Why?
- ILLUSTRATIONS For each of the given proteins: Draw the final location of the following proteins after being translocated. Label the organelle (as well as the organelle parts/compartments) and the cytosol (if necessary) in order to clearly depict the protein's location and orientation. Label the amino and carboxyl ends of the protein. Below your drawing, indicate: . . a. the receptor/s b. the energy source c. if there is signal peptide cleavage or none E. Mitochondrion H₂N-MTS ITS* "Internal targeting sequence that has no cleavage site -COOH SALEHere is a putative peptide sequence (position number on top of residues): 1 2 3 4 5 6 7 8 9 10 11 12 13 NH2- G C G N V T H N Q C V L S -COOH If expressed in a eukaryotic cell (please mark your answer in the blank space): Position(s) ___ could be N-glycosylated Position(s) ___ could be modified with myristic acid and the bond formed would be a ______________ Position(s) ______and _____ could be modified with palmiti c acid and the bond formed would be a ______________ Positio n(s) ________ could be a segment of a lipid-linked protein with a farnesyl anchor and the bond formed would be a ______________ Position(s) ________ could be a segment of an O-glycosylated protein Position(s) ________ could be modified with a glycosylphosphatidylinositol (GPI) anchor Position(s) ________ could be phosphorylatedUsing the the enzyme acid hydrolase in the lysosome: What is the final destination in which the protein will function? Which features will the protein receive during its manufacture? What is the primary structure (general)? Where is the primary structure made? Where are the secondary and tertiary structures made? Will the protein travel through any organelles during its manufacture? Which ones? What would be the overall result if some part of the manufacture process went wrong, such that the protein ended up as nonfunctional?
- . In the early days of ribosome research, before the exact role of ribo- somes was clear, a researcher made the following observation. She could find, in sedimentation experiments on bacterial lysates, not only 30S, 50S, and 70S particles but also some particles that sedi- mented at about 100S and 130S. When she treated such a mixture with EDTA, everything dissociated to 30S and 50S particles. Upon adding divalent ions, she could regain 70S particles, but never 100S or 130S particles. (a) Suggest what the 100S and 130S particles might represent, in light of current knowledge of protein synthesis. What important dis- covery did the researcher miss? (b) Why do you think reassociation to 100S and 130S particles did not work?please draw a cysteine - lysine mechanismLysozyme cleaves between NAG and NAM residues in bacterial cell walls and is, therefore, classified as a(an) O A. salt bridge, oxidoreductase O B. peptide bond; hydrolase OC. glycosidic linkage; oxidoreductase O D. glycosidic linkage, hydrolase O E. peptide bond; transferase