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…

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter4: Cells

Section: Chapter Questions

Problem 1ITD

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1. Amino acid side chains act as nucleophiles and proton donor/acceptors in various enzymatic reactions. We will use them frequently in reactions during 40B and therefore the purpose of this exercise 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. a. Gay-The Phe-The-Ser Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gily Gin-Ala-Ala-auhe-s NH C. For example: -Ser- will be represented by Gu Phe-lle Ala-Trp -Leu-Val-Arg-Gly Arg Gly-OH Add above the tree-letter code of each amino acid the relevant functional group on its side chain. OH Ser The protonation state of each functional group depends on the pH of the solution. Assume that Ozempic is in a solution at pH=7. Draw the functional groups at their correct protonation form. O Gu Phe-le- Ala-Trp Leu-Val- Arg-Gly Arg-Gly-OH Quay Thr Phe Thr-Ser…
Protease enzymes cleave proteins by hydrolyzing peptide bonds. The strategy for each type of metalloprotease begins with generating a nucleophile that attacks the peptide bond that attacks the peptide carbonyl group. O Macmillan Learning On the basis of the information provided in the figure, show the next step in the mechanism for peptide-bond cleavage by a metalloprotease. Metalloproteases H R₁ HN Zn Enz 2+ R₂ Draw curved arrows on the pre-drawn structures to show the metalloprotease mechanism. If you need to reset the structures, click More followed by Reset Drawing. Select Draw Templates Groups More B - H Enz H H с R1 | : HN O | Zn 2+ B R2 N Zn Erase
3CLpro is a cysteine protease, which are among the most common proteases in biochemistry, however they are a structurally diverse family of enzymes especially in the organization of the active site amino acids. A group of scientists have reported a potential drug molecule based on a binding study using circular dichroism. They report that the molecule binds to the active site. Can the experiment support the claims, why or why not? Which techniques might be used to support this claim?
A mixture of Aspartic Acid (pl 2.98), Histidine (pl 7.59), Lysine (pl 9.74), Phenylalanine (pl 5.48) and Threonine (pl 6.53) are separated by cation exchange chromatography. What is the order of elution of these amino acids if you use gradient buffer system from pH 10 to pH 2. v First 1. Aspartic Acid v Second 2. Histidine v Third 3. Lysine 4. Phenylalanine v Fourth 5. Threonine v Fifth 6. No separation
Why is the covalent intermediate of elastase stable at low pH? The catalytic histidine cannot act as general acid when protonated. O The catalytic histidine cannot act as a general base when protonated. The catalytic serine cannot form a covalent bond to substrate if the pH is below 7.4. O The catalytic serine cannot preferentially form a hydrogen bond with the catalytic histidine at acidic pH, causing these residues to shift out of their catalytically optimal positions.
H CH₂ H₂C HC-CH3 CH₂ H H₂C (S) H₂C H CH₂ CH₂ CH₂ NH O C NH NH₂ a) Which of the following statements about this peptide are correct? Group of answer choices Treatment of this peptide with trypsin generates two products. This peptide is a substrate for carboxypeptidase A Treatment of this peptide with cyanogen bromide generates a pentapeptide and a tripeptide. Treatment of this peptide with chymotrypsin generates three products. Treatment of this peptide with elastase generates 2 products. None of the above statements are correct. b) What is the sequence of this peptide using one letter abbreviations? c) What is the pH which would correspond to the ionization of the peptide as drawn above? 1, 5, 7, 10, 14
With regards to arganine illustrate the pH-dependent transitions on a titration graph from most to least protonated. Indicate also the relevant part of the amino acid which is associated with the transition on that part of the graph.
One of the reasons for oxidizing the disulfide bonds in RNase A before removing the urea in the Anfinsen experiment was to demonstrate that ... Urea promotes disulfide bond exchange O Incorrectly-folded proteins lose their enzymatic activity. Urea prevents disulfide bond formation. Urea forms thio-esters with reduced cysteines at pH 8.2 Disulfide bonds are required for enzyme activity.
Histidine is frequently used as a general acid or base in enzyme catalysis. Considering the pKa value of the side chain, suggest a reason why is this so?
1.Ala-Phe-Lys-Val-Val-Glu From the above polypeptide, what amino acid/s go/goes inside the cell after the following treatment: Chemotrypsin, thermolysin, then finally pepsin. What protein is left undigested? Write the primary structure of the undigested protein? 2.K-V-F-W-P-L-A-Y a.Chemotrypsin treatment b.Trypsin treatment c.Pepsin treatment d.Thermolysin treatment 3.Total acid hydrolysis of a pentapeptide complemented by total alkalinehydrolysis yields an equimolar mixture of 5 amino acids listed alphabetically, ala-cys,lys,phe,ser. N-terminal analysis with phenylisothiocyanate (PITC) generate PTH-ser. Trypsin digestion produces a tripeptide where N-terminal residue is cys and a dipeptide with ser as its N- terminal.Chemotrypsin digestion of the above tripeptide yields ala plus another dipeptide. A.What is the amino acid sequence of the tripeptide B.What is the amino acid sequence of the dipeptide derived from trypsin digestion? C.What is the primary structure of the original…
5. Consider the reaction for assembly of a tetrapeptide from for amino acids: Serine + Proline + Alanine + Methionine ----> SPAM tetrapeptide Is this reaction anabolic or catabolic? Is this a positive or negative delta G reaction? List at least three other terms you could use to describe this reaction. 6. Consider the reaction: Glutamic acid + Ammonia + ATP ----> Glutamate + ADP + Pi Is this reaction anabolic or catabolic? Is this a positive or negative delta G reaction? This is actually an example of a coupled reaction! Briefly, explain why reaction coupling is required, and how it works in this example.
1. Depict the structure features in the active site of cysteine protease 2. provide a step-wise reaction mechanism to show the hydrolysis of the peptide bond catalyzed by a cysteine protease

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