Concept explainers
(a)
Interpretation:
Histidine at
Concept Introduction:
On electrophoresis, the amino acids which contains net positive charge will move towards the negative electrode and the amino acids which contain net negative charge will move towards positive electrode.
(b)
Interpretation:
Lysine at
Concept Introduction:
On electrophoresis, the amino acids which contains net positive charge will move towards the negative electrode and the amino acids which contain net negative charge will move towards positive electrode.
(c)
Interpretation:
Glutamic acid at
Concept Introduction:
On electrophoresis, the amino acids which contains net positive charge will move towards the negative electrode and the amino acids which contain net negative charge will move towards positive electrode.
(d)
Interpretation:
Glutamine at
Concept Introduction:
On electrophoresis, the amino acids which contains net positive charge will move towards the negative electrode and the amino acids which contain net negative charge will move towards positive electrode.
(e)
Interpretation:
Glu-Ile-Val at
Concept Introduction:
On electrophoresis, the amino acids which contains net positive charge will move towards the negative electrode and the amino acids which contain net negative charge will move towards positive electrode.
(f)
Interpretation:
Lys-Gln-Tyr at
Concept Introduction:
On electrophoresis, the amino acids which contains net positive charge will move towards the negative electrode and the amino acids which contain net negative charge will move towards positive electrode.
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Chapter 27 Solutions
Organic Chemistry
- The isoelectric point (pl) of phenylalanine is pH 5.5. Draw the structure of the major form of glutamic acid at pH values of (a) 1 (b) 5.5 (c) 11.0.arrow_forward(a) Draw a structural formula for the products formed when alanine is treated with the following reagents. (i) (Boc)20, NaOH (ii) CbzCI, NazCO3 (iii) 2-Methylpropene, p-TSOH (b) Enfuvirtide, a 36-amino-acid peptide drug, was manufactured at a multi-tonne per year scale. The manufacture relied on solid phase synthesis with Barlos resin as the solid support. Part of the solid phase synthesis is shown below. Write the structure of the product A and discuss the cleavage mechaniśm of the peptide from the resin. 1. Fmoc-Leu-OH, DIPEA 2. 20% piperidine in DMF 3. Fmoc-Glu('Bu)-OH, HBTU, HOBt 4. 20% piperidine in DMF 5. Fmoc-Leu-OH, HBTU, HOBT 6. 20% piperidine in DMF 7. Fmoc-Leu-OH, HBTU, HOBE 8. 20% piperidine in DMF 9. 10% HOAC in CH2CI2 Barlos resinarrow_forwardConsider the following peptide : Phe – Glu – Ser – Met and Val – Trp – Cys – Leu. Do these peptides have different net charges at (a) pH 1? (b) pH 7? Indicate the charges at both pH valuesarrow_forward
- Answer the (b) part of the question 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-Glyarrow_forwardAn enzyme catalyzes the hydrolysis of an ester with a certain activity, but this activity is lost in a 3 M urea solution. What is the most likely explanation for the loss of activity? (A) Urea binds to the active site of the enzyme competitively with the substrate. (B) Urea causes the cleavage of the peptide bonds in the enzyme. (C) Urea causes the enzyme to denature and lose its specific three-dimensional shape. (D) Urea reacts with disulfide bonds in the enzyme.arrow_forward11. The structures of three amino acids are given below : NH2 0 Но -CH,CH-C-OH HOOCCH2CH2CH(NH2)COOH (1) (II)arrow_forward
- indicate the RIGHT alternative: (a) The Zwitterion form of an amino acid exists only at a point pH value. (b) In a peptide bond there is free rotation at the C-N bond. (c) In a polypeptide, the terminal carboxyl group may be present in its amide form. (d) At a pH greater than pI, an amino acid tends to move towards the cathode in an electrophoresis. (e) At any pH below pI, the predominant form of an amino acid is negatively charged.arrow_forwardThe amino acids in which the R groups have a net positive charge at pH 7.0 are (A) Lysine, Arginine, Histidine (B) Lysine, Aspargine (c) Histidine, Aspargine (D) Glutamine, Argininearrow_forwardDo the following compounds migrate to the cathode or to the anode on electrophoresis at the specified pH? Q.)Glutamic acid at pH 4.0arrow_forward
- Draw a structural formula for the form of amino acid most prevalent at pH 1.0. (a) Threoninearrow_forwardThe amino acid cysteine has three ionizable groups with the indicated pKas values. Draw the shapes of the amino acid at each of the following pHs: (a) 12 (b) 1 (c) 8 (d) 3arrow_forwardDetermine the isoelectric point of glutamic acid.(a) Draw the chemical structures of the amino acid in the pH ranges that you will use for the determination of pl.(b) Show all calculations for determining the pl of glutamic acid.arrow_forward
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