1. Amino acid side chains act as nucleophiles and proton donor/acceptors in various enzymaticreactions. We will use them frequently in reactions during 40B and therefore the purpose of thisexercise is to review the properties of amino acid side chains you have learned in 40A.Ozempic is a medication used for the treatment of type 2 diabetes and an anti-obesity treatment.Ozempic is a modified peptide that mimics the structure of the natural hormone GLP-1.H-His-N GAU-GH₂C CH₂Glu-Gly-Thr-Phe-Thr-Ser Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gly Gin-Ala-Ala-a.NHH-His-noH₂C CH₂au PhoPhe-lle Ala Trp Leu-Val-Arg Gly Arg-Gly-OHAdd above the tree-letter code of each amino acid the relevant functional group on its side chain.OHIFor example: -Ser- will be represented by SerNHOHb. The protonation state of each functional group depends on the pH of the solution. Assume thatOzempic is in a solution at pH=7. Draw the functional groups at their correct protonation form.Gu-GyGlu-Gy-Thr-Phe-Thr-Ser-Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gly-Gin-Ala-Ala-Gu Phe-Phe-lle Ala-Trp Leu-Val-Arg-Gly-Arg-Gly-OHOHC. What will be the protonation state of the long non-peptide side chain at pH=7?

Ozempic works like a little coach for your body, helping fight high blood sugar in type 2 diabetes.…

Answered: 1. Amino acid side chains act as…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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6. A. List all of the ionizable functional groups that are found in insulin when in aqueous solution. List which amino acid residues have these ionizable groups and list all of the pka and pKb values (including the R groups) that are on both polypeptide chains that make up insulin. (see the table at the end of this HW set; note that tyrosine and cysteine both have unusual pka's, since these side groups ionize above the pKR's given to have a negative charge). B. The isoelectric point of insulin is reported to be around 5.3-5.35. Using the method covered in class, estimate the isoelectric point of insulin and compare your answer to the values above. C. For a polypeptide to be soluble in an aqueous solution, is it good to be near the isoelectric point? Why or why not? Notes: a couple of unusual R group's that ionize (cysteine and tyrosine have R groups that have pka values; histidine has a pkb). The table at the end of this homework set (also in the lecture notes) lists the pka's and…
Amino acids are linked through peptide bonds to form proteins. This linkage of amino acids in the formation of proteins accomplished by [ Select ] reaction V [ Select ] Hydrolysis Fission Condensation Fusion
7. Chalcone isomerase catalyzes the reaction illustrated below. A series of modification experiments were performed on this enzyme to identify which amino acid residues might be in the active site and which might promote the cyclization reaction. OH Ho. Но Explain the following results: A) Acetic anhydride treatment inhibited enzyme activity. B) Pyrocarbonate inhibited activity and was found to modify 7 residues. However, this enzyme only contains 6 His and modification of these did not affect activity. C) lodoacetate inhibited activity but this effect coult be decreased in the presence of substrate or product. D) Methane methanethiol sulfonate modified the enzyme but did not inhibit catalytic turnover. In addition, this modification was reversed in the presence of B-mercaptoethanol. keNyons Rengent
Can someone please help me with these two questions, please hurry I only have 45 minutes;
1. Acid phosphatases are an important group of enzymes that can be detected in human bloodserum. Under slightly acidic conditions (pH 5.0), this group of enzymes can hydrolyzebiological phosphate esters as follows:R-O-P-O3-2 + H 2O R-OH + HO-P-O3-2.Acid phosphatases are produced and can be detected in erythrocytes, kidney, spleen, the liver,and prostrate gland. The enzyme from the prostrate gland is clinically important because anincreased activity in the blood is frequently an indication of cancer of the prostrate gland.Tartrate ion can strongly inhibit the phosphatase from the prostrate gland, but not acidphosphatases from other tissues. How can you use the information above to develop a specificprocedure for measuring the activity of the acid phosphatase of the prostrate gland in humanblood serum?
Cysteine proteases are enzymes that degrade proteins. You may have heard of some examples of these types of proteins before! Bromelain is an enzyme found in pineapple that is commonly used as a meat tenderizer and is the reason Jell-O with fresh pineapple will not solidify. Cysteine proteases are remarkably similar to serine proteases (like chymotrypsin), except they have a cysteine in their active site rather than a serine. Using the mechanism that we discussed for serine proteases, draw a corresponding mechanism for a cysteine protease cleaving the bond between an alanine-glycine dipeptide. Note that cysteine proteases do not require an aspartate in their active site. Also note that the cysteine is usually in its thiolate form (deprotonated) and the histidine is in its imidazolium form (fully protonated) in the resting state of the enzyme.
9. Bacteria can synthesize tryptophan, tyrosine, and phenylalanine through a series of biochemical reactions. All three amino acids are derived from the same precursor molecule, as shown in the diagram below. OH но OH Common Precursor Anthranilate Chorismate Synthase Mutase OH NH2 00 Trp Precursor Tyr/Phe Precursor a. A majority of this precursor is used by the enzyme chorismate mutase to synthesize another precursor that is used to make phenylalanine or tyrosine. Experimental data shows that when there is a high concentration of phenylalanine in a cell, more tryptophan is produced. This data also suggests that phenylalanine binds to chorismate mutase but does not bind to the enzyme's active site. Use what we learned in class to describe how this binding could regulate chorismate mutase's activity and result in more tryptophan being produced. b. The common precursor is also a substrate for a second enzyme, anthranilate synthase. The product of that reaction is a precursor for…
(d) of glucose oxidation in diabetic human patients treated with Metformin (●) and in (nondiabetic) control human patients (0). At –150 min both groups of subjects were started on an intravenous feed of 3-(®H)-glucose, and at t = 0 min they were started on an oral glucose tolerance test whereby a measured amount of glucose in water (a syrupy mixture) was swallowed followed by measure- ment of blood glucose levels at 30 min intervals. The flux of glucose oxidation was measured by the appear- ance of 3H2O in the blood stream. While the information The diagram to the right compares the rate 8000 ORAL GLUCOSE 6000- 4000- 2000- -120 -60 60 120 180 240 300 Minutes cannot be directly extracted from the reaction mecha- nism diagrams in the textbook, the glycolytic step in which the tritium is first released into water is that catalyzed by TPI, as illustrated at the beginning of Question #3. Explain why this step is suitable for measuring the flux of glycolysis through the release of °H…
1. In the mechanism of action of triose phosphate isomerase, Lys12 is an essential amino acid in the flexible phosphate gripper loop that undergoes a large conformational change to trap the substrate in the active site excluding water and holding the phosphate group in the correct geometry for isomerization rather than dephosphorylation. What would be the effect of the mutation of Lys12 to the unusual amino acid shown below? Explain. protein backbone
The following amino acids that are often found inside globulin molecules are () A, Tyr B, Phe C, Asn D, Glu True of false 1. In the de novo synthesis of purine nucleotides and pyrimidine nucleotides, base rings are first synthesized and then corresponding nucleotides are formed with phosphoribose. () 2. Transcription is the process of transferring genetic information from DNA to RNA. DNA is synthesized under the catalysis of RNA polymerase, and the direction of synthesis is from the 5 'end to the 3' end. () 3. The change of protein conformation is caused by the breaking of covalent bonds within the molecule. () 4. In very high and very low pH solutions, amino acids exist mainly in non-ionic form. () 5. The active center of an enzyme usually consists of several amino acid residues adjacent to each other in the primary structure. ()
I lea the - Oligopeptide 2 a. Give the three-letter and one-letter names of the amino acids in each oligopeptide starting from the amino terminal to the carboxyl terminal. Make sure that the amino acid names are arranged in CORRECT order for both oligopeptides. I b. After complete hydrolysis, which oligopeptide will yield more ATP molecules? How many NADH and FADH2 molecules will be theoretically produced? Show all relevant computations for each oligopeptide. Tabulate your answers to keep your answers organized. ( Oligopeptide Net ATP molecules Net NADH produced Net FADH2 produced produced Oligopeptide 1 Oligopeptide 2
7. During amino acid catabolism, how is amino group removed and excreted in the form of urea? Please write the reactions starting from a generic amino acid to the formation of urea. Please indicate the names of enzymes, cofactors, names of substrates, and products of each reaction and the location of the reaction i.e. whether in cytoplasm or mitochondria.

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