Interpretation:
The number of ATP equivalents consumption during the synthesis of the rhodanese polypeptide chain from its constituent amino acids needs to be determined.
Concept Introduction:
Amino acids are organic compounds containing amino as well as acidic groups. The general molecular formula of an amino acid is as follows:
Here, R refers to the different group for different amino acids. If there is more than one amino group present in an amino acid, they are considered as basic amino acids and if there is more than one carboxylic group, then they are considered as acidic amino acids.
![Check Mark](/static/check-mark.png)
Explanation of Solution
Elongation of the amino acid needs 4 ATP per amino acid. The initial step in elongating the polypeptide activates the amino acids and then it is connected to the tRNA. This procedure converts an ATP to an AMP, costing two phosphate groups. This is equal in hydrolyzing two ATPs in this step.
Subsequent, the “loaded” aminoacyl-tRNA is moved towards the ribosome’s A-site. This is achieved with the aid of the elongation factor EF-Tu and the GTP’s hydrolysis. The GTP hydrolysis is actively equal to hydrolyzing another ATP.
Lastly, the aminoacyl-tRNA is moved to the P-Site from A-site utilizing EF-G: GTP complex. Again, GTP is hydrolyzed to the GDP which is again equivalent to the single GTP hydrolysis. Thus, there are total 4 ATP equivalents per amino acids.
We now should consider termination and initiation. Initiation needs 2 ATP. One is in the form of GTP, for Met-tRNAi binding to form the 40S pre-initiation complex, and another is in the form of ATP in forming the initiation complex. The Met-tRNAi formation costs another 2 ATP.
Termination needs the hydrolysis of a single GTP. This means that for the amino acid, which is about 296 amino acids long, 4 ATP equivalents would be consumed within initiation, 1180 ATP equivalents are consumed during elongation, plus 1 ATP equivalent are consumed during termination. In this process, total 1185 ATP equivalents are provided.
Want to see more full solutions like this?
- Instruction for the said activity: Write the structure of each of the following peptide at pH7 and identify how many peptide bond in each number. d. Alanyl-phenylalanine- aspartate- cysteine e. Threonyl- Isoleucyl-methionyl- leucine f. Lysyl-alanine -Phenylalanyl-tyrosyl- serinearrow_forwardNeed help The β chains of HbA and HbS were treated with trypsin, and the sequence of the N-terminal tryptic peptides are as given below. Do these peptides separate from each other in an electric field if the pH is 7.0? Explain in detail the reasoning behind your answer and include your calculations for the charge of each peptide in your answer. HbA: Val-His-Leu-Thr-Pro-Glu-Glu-Lys HbS: Val-His-Leu-Thrarrow_forward11:14 structure. They provide the matrix or ground substance of extracellular tissue spaces in which collagen and elastin fibers are embedded. Hyaluronic acid, chondroitin 4-sulfate, heparin, are among the important glycosaminoglycans. 10. Glycoproteins are a group of biochemically important compounds with a variable composition of carbohydrate (1-90%), covalently bound to protein. Several enzymes, hormones, structural proteins and cellular receptors are in fact glycoproteins. Chapter 2: CARBOHYDRATES SELF-ASSESSMENT EXERCISES I. Essay questions 1. Define and classify carbohydrates with suitable examples. Add a note on the functions of carbohydrates. 2. Describe the structure and functions of mucopolysaccharides. 3. Give an account of the structural configuration of monosaccharides, with special reference to glucose. 4. Discuss the structure and functions of 3 biochemically important disaccharides. 5. Define polysaccharides and describe the structure of 3 homopolysaccharides. III. Fill…arrow_forward
- Part C Calculate to three decimal places the charge on a-melanotropin at pH value of 5. Express your answer using three decimal places. VE ΑΣΦ Submit Request Answer Part D Calculate to three decimal places the charge on a-melanotropin at pH value of 1. Express your answer using three decimal places. VE ΑΣΦ Submit ? Request Answer ?arrow_forwardProperties of an Enzyme of Prostaglandin Synthesis.Prostaglandins are a class of eicosanoids, fatty acid derivatives with a variety of extremely potent actions on vertebrate tissues. They are re-sponsible for producing fever and inflammation and its associated pain. Prostaglandins are derived from the 20-carbon fatty acid arachidonic acid in a reaction catalyzed by the enzyme prostaglandin en-doperoxide synthase. This enzyme, a cyclooxygenase, uses oxygen to convert arachidonic acid to PGG2, the immediate precursor of many different prostaglandins (prostaglandin synthesis is described in Chapter 21). a)The kinetic data given below are for the reaction catalyzed by prostaglandin endoperoxide synthase. Focusing here on the first two columns, determine the Vmax and Km of the enzyme. b)Ibuprofen is an inhibitor of prostaglandin endoperoxide synthase. By inhibiting the synthesis of prostaglandins, ibuprofen reduces inflammation and pain. Using the data in the first and third columns of…arrow_forwardAssignment on KetohexosesConstruct the structure of the following enantiomers or mirror images:1. D and L Fructose2. D and L Allulose3. D and L Sorbose4. D and L Tagatosearrow_forward
- whether a protein can to work in the same way in two different types of cells and if it possible that the same protein might function in different biochemical pathways in eye cells and muscle cells even if the protein's basic mechanism always remains the same. MAarrow_forwardhow the structure of arachidonic is suited for the synthesis of PGG2.arrow_forwardHydropathy & Amphipathicity 2 -1 -2- 110 210 310 410 510 Residue Number C. Draw the topology of this membrane protein in the bilayer and indicate the range of residues forming transmembrane a-helices.arrow_forward
- . Separating Glycated Hb From Normal Hb (Integrates with Chapters 5and 6.) Human hemoglobin can react with sugars in the blood(usually glucose) to form covalent adducts. The a-amino groups ofN-terminal valine in the Hb b-subunits react with the C-1 (aldehyde)carbons of monosaccharides to form aldimine adducts, whichrearrange to form very stable ketoamine products. Quantitation ofthis “glycated hemoglobin” is important clinically, especially fordiabetic individuals. Suggest at least three methods by which glycatedHb (also referred to as HbA1c) could be separated from normal Hband quantitatedarrow_forwardThin Layer chromatography (TLC). Explain the biochemical principle behind the separation of carbohydrates molecules by TLC as performed in practical 5. Explain which properties molecules must have to travel a short and large distance, respectively. Ketohexose sugars can form 8 different stereoisomers. How many of those isomers can be distinguished and resolved by TLC as performed in the practical and why? no more than 100 words totalarrow_forwardCENTRAL DOGMA & STRUCTURE-FUNCTION RELATIONSHIPS IN PROTEINS You are a bacteriologist studying a pathogenic protein (the "BAD" protein) that contributes to diseases caused by Staphylococcus aureus. BAD functions as an aß heterodimer, and the a subunit (25kD) and ß subunit (75KD) are held together by an electrostatic interaction between K in the a subunit and D in the B subunit. You are trying to dissociate the BAD subunits to prevent pathogenesis in the bacteria. Which mutation would you make to prevent the BAD subunits from forming a dimer? Assume neutral pH. (A) introduce AAA → AGA point mutation in the a subunit gene (B) introduce GAC → GAG point mutation in the ß subunit gene (C) introduce GAT → CGT point mutation in the ß subunit gene (D) introduce two point mutations: AAG → GTG in the a subunit gene & GAC → CTC in the B subunit gene (E) introduce two point mutations: AAA → TGC in the a subunit gene & GAT → TGT in the B subunit gene second base in codon A TGT Cys TGC Cys TTT Phe…arrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
![Text book image](https://www.bartleby.com/isbn_cover_images/9781305577206/9781305577206_smallCoverImage.gif)