Q4. The estimated pką of hydroimidazolone's R group is 6.93. If the pK₁ (α-COOH) and pK₂ (α-NH3) ofhydroimidazolone remain unchanged from its parent amino acid, would the pl of hydroimidazolone be higher(more basic) or lower (more acidic) than that of arginine? Explain your reasoning.Accumulation of macromolecules chemically modified by the addition of MGO has been associated with manyage-related diseases, including cancer. Thankfully, mammalian cells have developed several enzymaticmechanisms to clear cytotoxic MGO from the cell. The principal detoxifying pathway found in the cytosol of allcells is the Glyoxalase (Glo) system, shown in figure 3 below. Using glutathione as a co-substrate, thispathway converts MGO to D-lactate which can ultimately be metabolized in peroxisomes.CH₂se gjyshH CH₂SHMethylglyoxal(MG)Glo3GSH ++NH₂D-LactateY-Glutamyl-L-cysteinylglycine(GSH)Glo2Non-enzymaticS-D-LactoylglutathioneGSНОx=x-***CH3HemithioacetalGlo1Enediol(ate) enzyme intermediatesFigure 3 - Reaction schemes for the glyoxalase enzymes. Image source: Honek, John F. "Glyoxalase biochemistry"Biomolecular Concepts, 2015 6(5-6), p. 401-414.

Amino acids are biomolecules in which an amino group and a carboxyl group are linked to the same…

Answered: Q4. The estimated pKa of…

Biochemistry

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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

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Problem 1P

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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.
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=0
Non-standard amino acids are derived from common amino acids by biochemical modifications. Please identify the chiral centers of given non-standard amino acids.
Which of the amino acid side-chains would you expect to be protonated (i.e. has not lost its proton) under neutral pH conditions? Include reasons supporting your prediction.
Modify isoleucine to show the predominant forms at pH 1, 7, and 13. Isoleucine has pk, values of 2.4 (carboxyl group) and 9.7 (alaing group). Isoleucine at pl! 7 Isoleucine at pH I 대표 대, 1 - Isoleucine at pli 13 1 1 CH4. I I - CH I ## - 10 II
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).
please help me understand asap Please draw by hand a tripeptide of Glu, Gln, and 1 amino acid of your choice (Not Glu or Gln again) at pH 7.0 and 9.0. The only requirement is that the amino acid should be 1 of the amino acids with ionizable R groups. Peptide should have appropriate charges on groups. Please
32
Suppose you have a solution of a protein, which contains a specific Tyr residue that has an actual (measured) pKa of 8.8. The protein binds a ligand by several noncovalent interactions, one of which is a hydrogen bond in which the Tyr phenolic hydroxyl group must serve as a hydrogen bond donor. Calculate the percentage of the protein molecules in which that tyrosyl residue's phenolic hydroxyl group could serve as a hydrogen bond donor at pH 8.5
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
Hi, please help with this question: What is the net charge on the amino acid cysteine at pH 8.0? (pKa values are α-carboxyl 2; α-amino 10; side chain 8) Thanks

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Q4. The estimated pKa of hydroimidazolone's R group is 6.93. If the pK₁ (α-COOH) and pK₂ (α-NH3) of hydroimidazolone remain unchanged from its parent amino acid, would the pl of hydroimidazolone be higher (more basic) or lower (more acidic) than that of arginine? Explain your reasoning.