7Now consider three sugars-glucose, glucuronic acid, and N-acetylglucosamine. Use shorthand (e.g., Glc?(1?4)GlcUA?(1?4)GlcNAc) to represent 10 trisaccharides with the sequence Glc?GlcUA?GluNAc. Check all that apply.Glcß(14) GlcUAB(1 → 6) GlcNAcGlca (13)GlcUAa(1→3)GlcUAa(1 → 4)GlcNAcGlca (14) GlcUAB(16) GlcNAcGlcß(44) GlcUAa(44)GlcNAcGlca(14) GlcUAB(1 →4)GlcUAß(1 → 3) GlcNAcGlca(15) GlcUAa(14) GlcNAcGlcß(14) GlcUAa(5 → 1) GlcNAcGlca (12) GlcUAB(13) GlcNAcGlca (1 → 2)GlcUAa(1 → 3)GlcNAcGlca(11) GlcUAa(11) GlcNAc□ Glcß(1 → 5)GlcUAß(1 → 5)GlcNAcGlca(1 → 2) GlcUAß(1 → 4)GlcNAcGlca(14) GlcUAa(14) GlcNAcGlcß(13) GlcUAB(1→ 4)GlcNAcGlcß(14) GlcUAB(14) GlcNAcSubmitMy Answers Give Up

A glycosidic bond is formed between 2 carbon atoms as the result of a dehydration reaction. The…

Answered: Now consider three sugars-glucose,…

Now consider three sugars-glucose, glucuronic acid, and N-acetylglucosamine. Use shorthand (e.g., Glc?(1?4)GlcUA?(1?4)GlcNAc) to represent 10 trisaccharides with the sequence Glc?GlcUA?GluNAc.

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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Modify isoleucine to show the predominant forms at pH 1, 7, and 13. Isoleucine has p?ap�a values of 2.4 (carboxyl group) and 9.7 (amino group).
Complete multiple choice
2. | Calculate the overall charge (pH 7) on the following three polypeptides and answer the questions below. Assume the following pKa values: N-terminal -NH3®, 7.0; all -COOH groups, 4.0; Arg, 12.5; Cys, 8.4; His, 6.0; Lys, 10.0; Tyr, 10.0. (A) Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-Gly-Lys-Lys-Arg-Arg-Pro-Val-Lys-Val-Tyr-Pro-Asp-Ala -Gly- Glu-Asp-Gln- Ser-Ala-Glu-Ala-Phe-Pro-Leu-Arg-Glu-Phe (B) Ser-Tyr-Ser-Met-Glu–His-Phe-Arg–Trp–Gly-Ala-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu–Val-Tyr-Pro-Asp- Ala-Gly-Glu-Asp-Gln-Ser-Ala-Glu-Ala-Phe-Pro-Leu-Glu-Phe-Cys-Ser-Tyr-Ser-Met-Glu-His-Phe-Asp-Trp-Gly- Asp-Pro-Val-Gly-Pro-Asp-Ala-Gly-Asp-Gln-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu-Val-Tyr-Pro-Asp-Ala | (C) Gly-Ser-Val-Arg-Asp-Pro-Val-Lys-Glu–Val-Tyr-Pro-Asp- Lys-Ala-Gly-Arg-Glu-Ser-Arg-Ala (a) Which of the three peptides would elute first from a gel filtration column? (b) Which of the three peptides would migrate the fastest on SDS-PAGE (c) Which of the three peptides could be…
5) In the below two step transformation, the first step AG is positive i.e. 1.7 kJ/mol. Yet this two step coupled reaction takes place to form Fructose-1.6-bisphosphate. Explain why?" C-H CH-OH CH,-0 H-C-OH AG"- 1.7 KJ/mol (+0.4 kcalmol) C=0 AG"=-14.2 k/mol(-3.4 kcalmol) HO-C-H HO-C-H HO-C-H H-C-OH H-C-OH H-C-OH H-C-OH H-C-OH ATP ADP H-C-OH CH-0-P. CH,-0-P-o- CH,-o- Glucose-6-phosphate Fructose-6-phosphate Fructose-1,6-bisphosphate
a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).
1 Draw the following polypeptide: Met- Tyr-Val-Ser-Asn 2A Draw the hydrolysis of a dipeptide consisting of phenylaline and glutamic acid. 2B What are the fuctional group present in the side chains of the amino acids.( phenylalanine and glutamic acid) 2C are the sidechains in part 2B hydrophobic or polar 2D where would you expect to find them ( surface or interior of a protein) ? why ?
5. + H OH H Кон H X OH Upon acid Almost 30% of the cocoon of the parasitic beetle Larinus maculatus consists of the carbohydrate trehalose. Trehalose was subjected to exhaustive methylation, which hydrolysis, trehalose gives D-glucose as the only product. converts all available OH groups to OCH3 groups; this was and releases the methyl groups from all anomeric carbons followed by mild hydrolysis in acid which breaks the linkage without affecting any other OCH3 groups in the structure. Following exhaustive methylation and subsequent hydrolysis of trehalose with aqueous acid, only one product, 2,3,4,6- tetramethylglucose, is obtained. trehalose? What is the structure of Demonstrate that your proposed structure is consistent with the data presented above. OH
4 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
6 (a) A decapeptide has the following amino acid composition: Ala2 , Arg, Cys, Glu, Gly, Leu, Lys, Phe, Val Partial hydrolysis yields the following tripeptides: Cys-Glu-Leu + Gly-Arg-Cys + Leu-Ala-Ala+ Lys-Val-Phe + Val-Phe-Gly. Reaction of the decapeptide with 2,4-dinitrofluorobenzene yields 2,4-dinitrophenylysine. From the experimental data, deduce the primary structure of the decapeptide. (b) Suggest a scheme you will follow to synthesize the dipeptide Ala-Gly
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
2. | Calculate the overall charge (pH 7) on the following three polypeptides and answer the questions below. Assume the following pKa values: N-terminal –NH3®, 7.0; all -COOH groups, 4.0; Arg, 12.5; Cys, 8.4; His, 6.0; Lys, 10.0; Tyr, 10.0. (A) Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys–Pro–Val–Gly–Lys–Lys–Arg-Arg-Pro-Val-Lys–Val-Tyr-Pro-Asp-Ala -Gly- Glu-Asp-GIn– Ser-Ala-Glu-Ala-Phe-Pro-Leu-Arg-Glu-Phe (B) Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Ala-Pro-Val-Gly-Glu-Glu–Cys-Asp-Pro-Val-Glu–Val–Tyr-Pro-Asp- Ala-Gly-Glu-Asp-Gln-Ser-Ala-Glu-Ala-Phe-Pro-Leu-Glu-Phe-Cys-Ser-Tyr-Ser-Met-Glu–His-Phe-Asp-Trp-Gly- Asp-Pro-Val-Gly-Pro-Asp-Ala-Gly-Asp-Gln-Pro-Val–Gly–Glu-Glu-Cys-Asp-Pro–Val-Glu–Val–Tyr-Pro-Asp-Ala (C) Gly-Ser-Val-Arg-Asp-Pro-Val-Lys-Glu-Val-Tyr-Pro-Asp- Lys–Ala-Gly-Arg-Glu-Ser-Arg-Ala (d) Which of the three peptides would migrate the closest to the anode in isoelectric focusing? (e) Which of the above peptides would elute last from a gel filtration column? (f) Which of the three…
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