Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 30, Problem 16P
The Energetic Cost of Peptide Elongation How many ATP equivalents are consumed for each amino acid added to an elongating polypeptide chain during the process of protein synthesis?
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Chapter 30 Solutions
Biochemistry
Ch. 30 - Prob. 1PCh. 30 - Prob. 2PCh. 30 - The Second Genetic Code Review the evidence...Ch. 30 - Codon-Anticodon Recognition: Base-Pairing...Ch. 30 - Consequences of the Wobble Hypothesis Point out...Ch. 30 - Prob. 6PCh. 30 - Prob. 7PCh. 30 - Prob. 8PCh. 30 - Prob. 9PCh. 30 - The Consequences of Ribosome Complexity Eukaryotic...
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- What is the smallest number of molecules of ATP and GTP consumed in the synthesis of a 200- residue protein, starting from amino acids? Assume that the hydrolysis of PP i is equivalent to the hydrolysis of ATP for this calculation.arrow_forwardunder certain conditions alpha helical bundles can form and can facilitate protein insertion into membranes. discuss how they coudl achieve this at a biochemical level?arrow_forwardStarting from glutamine + aspartate + glycine + CO + N-formyl-THF + ribose-5-P: How many ATP equivalents (GTP is an ATP equivalent) are required for the synthesis of the purine nucleotide ATP?arrow_forward
- Combustion of glucose (C6H12O6) is the main source of energy for animal cells: -> + C6H12O6s 602g + 6C02g 6H2O1 = \Delta Grxn37\deg C-2872.kJ One of the most important uses to which this energy is put is the assembly of proteins out of amino acid building blocks. The Gibbs free energy of formation of one peptide bond, joining one amino acid to another, is 21/kJmol. Suppose some cells are assembling a certain protein made of 88 amino acids. (Note that the number of peptide bonds in the protein will be one less than the number of amino acids.) Calculate the minimum mass of glucose that must be burned to assemble 150. \mu mol of this protein.arrow_forwardBriefly describe each of the following possible posttranslational protein modifications. Give an example of each. Cross-linkage glycosylation and phosphorylation cleavage assembly into polymeric proteins (> 1 polypeptide)arrow_forwardConsider a protein with two surface-exposed histidine residues: HisA is a “typical” histidine residue with a pKa = 6.2 HisB is involved in a stabilizing interaction (His-NH+ ..... -O2C-Glu) with a neighboring glutamic acid residue. For HisB, the Gibbs free energy of deprotonation at pH = 7.0 and T = 293K is ΔG'o = +15 kj mol-1. If you had a solution, at pH = 7.0 and T = 293K, containing this protein: a) What fraction of HisA residues are protonated? b) What fraction of HisB residues are protonated? c) What is the pKa of HisB?arrow_forward
- SDS-AGE analysis of protein for subunit composition: A protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography (gel filtration). When subjected to gel electrophoresis in the presence of SDS only and SDS plus 2-ME, the following pattern of SDS-PAGE is observed. MM - molecular standard proteins with known molecular weight (in kDa) as shown on the left of the gel are used to determine the size of unknown proteins. a) Determine the subunit composition of this protein (i.e., how many subunits are in its quaternary structure?). MM SDS SDS 2-ME kDa 180- 160- 100- 90- 60- 50-arrow_forwardThe major difference between a protein molecule in its native state and in its denatured state lies in the number of conformations avail- able. To a first approximation, the native, folded state can be thought to have one conformation. The unfolded state can be estimated to have three possible orientations about each bond between residues. (a) For a protein of 100 residues, estimate the entropy change per mole upon denaturation. (b) What must be the enthalpy change accompanying denaturation to allow the protein to be half-denatured at 50 °C? (c) Will the fraction denatured increase or decrease with increasing temperature?arrow_forwardGLUT 1 contains several amphipathic transmembrane hellices, each with Its polar face oriented towards the central cavity, producing a transmembrane channel available for interaction with glucose, as shown in the figure below. Which of the following sequences are most likely to form a transmembrane helix? Helical wheel diagram is given for reference. a Ser-Ala-Val-Phe-Thr-lle-Met O Phe-Leu-Val-Thr-Asn-Met-lle O Val-Ser-Thr-Val-Phe-Asn-Glu Ser-Asn-Leu-Asp-Gin-lle-Phe O Asn-Leu-Ala-Ser-Gin-Phe-earrow_forward
- Peptide sequence using 1-letter code for amino acids: EDLSMTCFRH What is the net charge of this peptide at pH 9? Use the pKa values from Table 4-1 from Voet, Voet and Pratt. -2 -1 O +1 +2arrow_forwardThe following peptide that has been acetylated at the C-terminus: CH3C(O)-GEEGH-NH2 Plot the titration curve for pH as a function of mols NaOH added, indicating the relevant pKa values and the pI value on the graph, label all axes appropriately.arrow_forwardA ribonuclease reaction containing 0.50µM RNASE A will hydrolyze RNA at a maximal rate of 5µM/s in the presence of 40mM RNA at 37°C. What is the turnover number, kcat, for the enzyme (per second).arrow_forward
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