6. ANSWER THE FOLLOWING PROBLEM AND EXPLAIN YOUR ANSWER FOR BETTER UNDERSTANDING. Fill in the blanks peptide bonds and In the peptide, HAPPYNEWYEAR, there are a total of 12 molecules of water were removed in its formation.(Write the symbol of the number)
Q: Identify the shape of the hemoglobin complex. tetrahedral pentadral hexadral heptadral octahedral
A: Red blood cells (erythrocytes) have presence of a protein which is known as Hemoglobin. Hemoglobin…
Q: -catalyzed, single-substrate reaction + S ring three conditions: [S] > Km. each statement with the…
A: Those proteins or biological catalysts which help to speed up the chemical reaction are termed…
Q: Draw the chemical mechanism (with electron-pushing arrows) for the addition of an RNA nucleotide…
A: The process by which m RNA is synthesized from DNA is known as transcription. RNA polymerases are…
Q: The reaction coordinate diagram shown below is for the mitochondrial enzyme ATP synthase. G KJ/mol…
A: A reaction coordination graph is a graphical representation of the free energy changes that occur…
Q: Label blood types O and B with the correct monosaccharides. The defining monosaccharide is noted by…
A: AB blood typing gives rise to 4 main types of blood groups, which are A, B, AB and O. There are 3…
Q: Frog muscle cells and the solution bathing the cells contain ions at different concentrations. The…
A: The concentrations of Na+, Ca2+, K+, and Cl- are shown in the following table. Temperature = 25…
Q: 2. You made a pH=9.8 buffer solution by mixing NaOH and glycine to give a solution that is 0.20 M in…
A: In order to solve (d), first we need to calculate (c). So, here is a brief and comprehensive…
Q: 10.32 Give an explanation for the Lineweaver-Burk plot for a certain enzyme-catalyzed reaction shown…
A: Michaelis Menten equation describes the mathematical relationship between initial rate of reaction…
Q: increase in AMP Increases glycolytic activity glucagon secretion feeding insulin secretion increase…
A: A metabolic process called glucose synthesis allows the body to produce glucose from…
Q: You run a series of assays at 25°C on enzyme A. You measure the velocity for a range of S…
A: This question can be solved using Lineweaver Burk plot. This graph also represents the enzyme…
Q: 2. ATP is our energetic molecule of choice! We should think about its structure and how it gets…
A: ATP is the energy currency that a cell spends on metabolic transactions. ATP is a nucleotide. Its…
Q: Calculate to three decimal places the charge on a-melanotropin at pH value of 5. Express your answer…
A: Net charge on the amino acid with negative side group: Net charge on the amino acid with positive…
Q: The pH of an aqueous solution containing fermentation nutrients with low buffering capacity should…
A: Fermentation is a critical process in biotechnology and the food industry that involves microbes…
Q: two of the three biopolymers and explain why these biopolymers are not good options for…
A: Polymers are long-chain molecules while biomolecules are molecules produced by biological entities,…
Q: ARTVIVGKSFSLGVDW. Calculate the number of charged groups in this peptide at pH 5. Use the provided…
A: There are seven amino acids with ionizable side chains. They are Glutamate (E), Aspartate (D),…
Q: Part B. Classify Fatty Acids as Saturated or Unsaturated 2. Identify each fatty acid below as…
A:
Q: How many oxygen atoms are reduced from each nadh and fadh
A: By the end of citric acid cycle most of the energy has been converted into high energy electrons in…
Q: Do the P-waves of different subjects have the same amplitude? The QRS complexes? The T-waves? Why?
A: The P-wave, QRS complex, and T-wave amplitudes can vary between individuals due to differences in…
Q: Inhibitors are compounds capable of blocking the catalytic process. Outline with the use of graphs…
A: Ezymes are the biocatalysts that increase the rate of reaction without changing itself to the…
Q: AGO
A: Gibb's free energy:It is denoted as ∆G.It is a fundamental thermodynamical concept.It measures a…
Q: For the reaction glutamate (aq) + oxaloacetate2- (aq) a-ketoglutarate²- (aq) + aspartate- (aq) the…
A: When temperature and pressure are held constant, the amount of work that can be done in a…
Q: An alpha-helix transmembrane protein has 35 amino acid residues embedded in a lipid bilayer…
A: The repeating unit of an alpha-helix is the helix turn. Each helical turn in alpha-helix has an…
Q: Myoglobin would be an inappropriate carrier of oxygen to peripheral tissues because: Myoglobin…
A: Hemoglobin and Myoglobin are two oxygen binding proteins found in mammals. Myoglobin is an oxygen…
Q: 19. Draw all 20 of the genetically encoded amino acids at (a) pH = 1; (b) pH = 1; (c) pH = 12.…
A: Amino acids are organic compounds that form the building blocks of proteins in cells. The structure…
Q: Transport of histidine into a bacterial cell was measured at several different histidine…
A: The kinetics of transport of a molecule via a carrier protein and a protein channel differ from each…
Q: Representations of sequencing chromatograms for variants of the a chain of human hemoglobin are…
A: The sequencig chromatograms given in question are generated as we conduct Automated DNA sequencing…
Q: Using a biochemical technique called site-directed mutagenesis, it is possible to substitute a…
A: Site-directed mutagenesis is a method employed in the lab to perform accurate and deliberate…
Q: Which is the best explanation of why kinesin doesn't bind covalently to its structural protein…
A: Kinesins are motor proteins responsible for transporting cellular cargo along microtubules within…
Q: After completing your analysis of the different bacterial methyltransferases at MethylTranspharmiX,…
A: Reversible enzyme inhibition can be of 4 types generally. They…
Q: write the one letter code for oligopeptide ser-cys-ille-glu-Asn-cys-glu and calculate the total…
A: Before calculating the total charge on the peptide, we need to be thorough with the principle behind…
Q: Consider a uniport system where a carrier protein transports an uncharged substance A across a cell…
A: The following equation describes the mathematical relation for the change in free energy () SHAPE…
Q: Enolase catalyzes the reversible reaction shown below. Draw the detailed mechanism for the reaction…
A: Enolase catalyzes the interconversion between 2-phosphoglycerate (2-PG) and phosphoenolpyruvate…
Q: Crocodiles can use virtually 100% of the oxygen in its blood, whereas humans can extract only about…
A: Let's evaluate each statement to determine which one best explains why HCO3 in the crocodile works…
Q: It is maintained by a bond with resonance structures. It will be disrupted by extreme pH conditions.…
A: A protein's biological function depends on its three-dimensional structure. The 3D structure is…
Q: Many drugs are competitive inhibitors of specific enzymes. For drugs that act as competitive…
A: When a substrate (S) binds to the active site of an enzyme (E), it leads to the formation of an ES…
Q: When electrons are removed from a food molecule,the moleculeis conducting anendergonic reaction.…
A: Endergonic reactions are reactions that require an input of energy (heat) to take place. Exergonic…
Q: The scientific name of the fructose molecule shown below is CH2OH OH НО ОН CH₂OH
A: Fructofuranose is a structure which is similar to the furan ring, which has a five carbon membered…
Q: Consider the last few minutes of a tough race, when the runner's energy reserves are depleted.…
A: Glycolysis is the process by which the glucose undergoes breakdown in the cell to convert into…
Q: Cofactors, coenzymes, and prosthetic groups datang une pomm
A: Enzyme function:Enzymes are the biological catalysts which speed up the reactions in organisms.These…
Q: Provide a reasonable step-wise mechanism for the reaction below, involving TPP as a coenzyme (can…
A: Enzyme catalysis can occur via different mechanisms such as general acid/base catalysis, covalent…
Q: In the absence of an enzyme, a reaction has a Keq = 10¹5. i. Is AGO for the reaction + or -? ii.…
A: In a general reaction such as:aA + bB ⇌ cC + dDAt equilibrium (steady state), the concentration of…
Q: Glucagon is a hormone that is released when the level of glucose in the blood is low. Glucagon uses…
A: Glucagon is secreted by the α cells of pancreas.Glucagon is a hormone that helps to regulate blood…
Q: Why is control of column and detector temperature more important for non- suppressed IC (Ion…
A: The control of column and detector temperature is a fundamental aspect of ion chromatography (IC), a…
Q: Which of the following runs an identical application as the production environment? Select one: Oa.…
A: The natural world that hosts living things is known as the environment. It consists of the…
Q: select the false statement regarding phospholipid bilayer membranes. phospholipid bilayer part…
A: A cell is made up of different biomolecules. Biomolecules are of four types: carbohydrates,…
Q: Complete the statement to make it true. Carbon monoxide binds to heme with a higher affinity than…
A: Complete the statement to make it true: Carbon monoxide binds to heme reversibly with a higher…
Q: Finish the sentence alpha helical secondary structures in proteins Are connected by beta- turns Are…
A: Secondary structure is the ordered arrangement or conformation of amino acids in localized regions…
Q: Use Excel to make the data plot and include the graph in your submission. For all questions…
A: Since you have posted a question with multiple sub parts, we will provide the solution only to the…
Q: Place all eight of these steps of the insulin signaling pathway in the correct order. The…
A: One essential biological mechanism controlling glucose absorption and metabolism is the insulin…
Q: Indicate how the observed Km of an enzyme would change in the presence of inhibitors having the…
A: The Km is known as Michaelis constant, it is the concentration of substrate at which reaction…
Step by step
Solved in 3 steps with 1 images
- 4. a. Give the full names of the amino acids in this peptide. НзN — CH—С-N—CH— С-N—CH—С—О ČH3 H ČH,OH H. CH2 -ОН b. Calculate the isoelectric point (pl) of a peptide with sequence SNARE. Show your work in a table, giving the pKa values of the ionizable groups, pH, and charges. Step marks are counted. Don't need to write “protonated" or “deprotonated".5. Refer to Model 2 for information relevant to this question. A sample of the peptide Lys-Glu-Ser has a net charge of zero between what two pH values? What is the pl of Lys-Glu-Ser? Model 2: The pl of a peptide is determined by examining the ionizable groups. The protonated and unprotonated forms of each ionizable group are in equilibrium. Consider the peptide Lys-Glu-Ser shown below at pH 7.2. The complete structure is on on the left and a stylized structure with just the ionizable groups is on the right. While the N-terminal is depicted as protonated, a sample of Lys-Glu-Ser is composed of a population of molecules and within that population some molecules contain a non-protonated N-terminal group at pH 7.2. may H3N* COO- H3N-CH-CIN-CH C N-CH C- H. pK 3.5 OH H. pK= 8.5 COO- CH2 CH2 CH2 NH, pK 10.0 pK 4.2 CH2 CH2 OH CH2 c=04 This is a three-part question about a tripeptide. Answer all three sub-questions. The pKR of side chains of Tyr, and Lys is 10.46 and 10.54 respectively. The molecular weight of amino acids Ala, Lys, and Tyr in neutral form is 89.1, 146.2, and 181.2 Da, respectively. 1) Draw the chemical structure of the dominant form of tripeptide AKY at pH = 11.5, ensure you have the correct stereochemistry and ionization state of each functional group (Hint, lysine has a C-epsilon as the furthest carbon from C-alpha). 2) Calculate the pI of tripeptide AKY, assuming the terminal amino group has a pKa of 8.0, and the terminal carboxyl group has a pKa of 3.5 3) Calculate the molecular weight of AKY at pI
- 1. a. Draw the following pentapeptide: lysine-leucine-aspartate-threonine-phenylalanine b. Label the amino and carboxyl terminus of your peptide c. Label each amino acid residue with one and three letter abbreviations d. Label the alpha carbons e. Label the bonds around which phi and psi rotational angles occur f. Which amino acid in this chain is most likely to be phosphorylated? Which amino acid is most likely to be acetylated?6. b. Draw a box around the disulfide bridge in oxytocin, if present, or write "none". 7. Mark each peptide bond in oxytocin by making the corresponding line in the structure thicker or marking it with a different color. The first one is shown for you as an example (in dark orange). 8. Number the central carbon of each amino acid in oxytocin by pointing a small arrow to it or by circling the corresponding vertex in the image. Numbers 1 and 2 indicate the central carbons of the first and second amino acids of oxytocin, and are shown for you as an example. 9. Fill out the following table, listing amino acids that make up oxytocin in order, from the N terminus to the C terminus, characterizing each amino acid by the properties of its R group (side chains), and briefly indicating the reasoning for the characterization. You may consult amino acid groupings by category in the slides (or the textbook, p.49), but you must explain the reasoning for each in your own words. CO 1 AA# Abbre- Full…7. A peptide has the sequence Cys-His-Glu-Met-lle-Ser-Thr a. Write out the single letter sequence of this peptide. b. What is the overall charge of the peptide? Is it acidic? Basic? c. Draw the chemical structure of the peptide at pH 7.0 and show any charged groups d. What is the classification of each amino acid in this peptide regarding polarity and charge? 8. The following proteins represent a wide range of molecular weights and isoelectricpoints. Mr is the molecular weight of a single protein chain. • Protein 1: Mr 68,544; pl 6.11 (monomer) • Protein 2: Mr 29,041; pl 5.32 (dimer) Protein 3: Mr 15,805; pl 5.7 (dimer) • Protein 4: Mr 12,165; pl 4.74 a. Which protein is the most acidic? Explain your answer. b. Which protein will migrate the slowest in an SDS-PAGE? Explain your answer. c. In what order will these proteins elute from a cation exchanger at phH 8? Explain your answer. d. In what order will these proteins salt out from a pH 7 solution by the dropwise addition of saturated…
- 1. An intrinsically disordered protein (IDP) is a protein that lacks a fixed three- dimensional structure. Estimate the size of an IDP of 100 amino acids by calculating the most probable end-to-end length of the protein. Assume the protein is a freely-joined chain with the length of each segment (amino acid) b = 3Å.1. Consider the peptides P-A-I-G-E and M-A-T-T. a. Draw the structure of each peptide at a pH of 7.0 b. Draw the structure of each peptide at a pH of 12.0 c. Calculate the pl of both peptides. Based on your answer, do you think these two peptides can be separated using ion exchange chromatography at a pH of 5? Explain.1. Consider the peptide with amino acid sequence NICE. a. Write the full name and the three-letter abbreviations of the amino acids in the реptide. b. Calculate the net charge of the peptide at pH 7.0. Show you work in a table. с. Calculate the pI of the peptide. Show you work in a table.
- 1. Draw the structural formula of the amino acid serine that predominates in solution at each of the following pH values. A. pH = 4.0 В. рH %3D9.0 С. рH %3D 7.0 %3D1.Describe in detail how to detect the primary structure of protein. 2.Given a mixture of lysine,histidine and cysteine.The isoelectronic point of the amino acids are as follows: histidine:7.64 lysine:9.74 cysteine:5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.5. The amino acid sequences of three peptide fragments are shown below. Peptide 1: QAMGRAGDLKYLGLHSV Peptide 2: ALMALFMVMALVLVSVLFIA Peptide 3: MVEDLLKQIARYLISE (a) Circle all of the charged residues in peptide 1 (assume pH = 7.0). Box all of the aromatic residues in peptide 2. Underline all of the nonpolar residues in peptide 3. (b) Determine the net charge of the predominant form of each of the peptides at pH 4.5 and pH 11.5. Assume the ionizable groups have the pKa values listed in Table 2.1 of your text. (c) Which of these peptides would be most likely to be found as an a helix in a soluble (cytoplasmic) protein? Which would be most likely to be found as an a helix in a transmembrane protein? Which would be least likely to form an a helix of any kind? Briefly explain your answers.