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) The isoelectric point (pI) of phenylalanine is pH 5.5. Draw the structure of the major form of phenylalanine at pHvalues of 1, 5.5, and 11.(b) The isoelectric point of histidine is pH 7.6. Draw the structures of the major forms of histidine at pH values of 1, 4,7.6, and 11. Explain why the nitrogen in the histidine ring is a weaker base than the a-amino group.(c) The isoelectric point of glutamic acid is pH 3.2. Draw the structures of the major forms of glutamic acid at pH valuesof 1, 3.2, 7, and 11. Explain why the side-chain carboxylic acid is a weaker acid than the acid group next to thea-carbon atomarrow_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
- (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_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_forwardWrite the complete structures for the following peptides. Tell whether each peptide is acidic, basic, or neutral.(a) methionylthreonine (b) threonylmethioninearrow_forward
- Q1)In the pH range 1.82 to 8.99, H2Arg+ is the principal form of arginine. Which is the second most prominent species at pH 6.0? At pH 5.0?Q2) (a) Draw the structure of the predominant form (principal species) of 1,3-dihydroxybenzene at pH 9.00 and at pH 11.00.(b) What is the second most prominent species at each pH?(c) Calculate the percentage in the major form at each pHarrow_forward11. The structures of three amino acids are given below : NH2 0 Но -CH,CH-C-OH HOOCCH2CH2CH(NH2)COOH (1) (II)arrow_forwardAnswer 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_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_forwardh) Specify the absolute (R/S) configuration of the amino group in structure IV. (i) If the substituents in structures I, IV and V were identical (all OH or all NH2), which structure would result in a meso compound? (j) If each hydroxy group for structures I, II and VI were replaced with another amino group, which compound would be made optically inactive?arrow_forwardWrite the complete structures for the following peptides. Tell whether each peptide is acidic, basic, or neutral.(a) methionylthreonine (b) threonylmethionine(c) arginylaspartyllysine (d) Glu-Cys-Glnarrow_forward
- Introduction to General, Organic and BiochemistryChemistryISBN:9781285869759Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar TorresPublisher:Cengage Learning