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Concept explainers
Interpretation:
Glutamic acid at low
Concept Introduction:
Many amino acids are linked together through amide bonds to form a biologically large molecule known to be proteins.
Amino
Zwitter ion has both positive as well as negative charge, thus it is also called neutral dipolar ion.
Zwitter ion accepts proton in acidic condition and in basic condition zwitter ion lose electrons.
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Chapter 18 Solutions
Pearson eText Fundamentals of General, Organic, and Biological Chemistry -- Instant Access (Pearson+)
- What is the net average charge on the predominant form of lysine at pH values of (a) 2.0, (b) 5.0 and (c) 7.0? CLUE: draw the structure of lysine and show its different charged forms; then consider in which pH domains the pKa values for deprotonation/protonation occur.arrow_forwardPhosphate buffers are commonly used to mimic biological systems. Given that phosophoric acid is a triprotic acid with three pKas (2.12, 7.21, and 12.32), why do you think this is? What are the dominant buffering compounds present in a phosphate buffer near physiological pH?arrow_forwardA peptide has the sequence: Glu–His–Trp–Ser–Gly–Leu–Arg–Pro–Gly1. What would be the net charge of the molecule at pH a) 3, b) 8, and c) 11? (Use pKa values. Do not calculate the value per se, but instead estimate considering only fully protonated, or deprotonated states. Then estimate the pI for this peptide. Show full, clear and complete procedurearrow_forward
- Are all the amino-acids soluble in water? Explain why?arrow_forwardThe skeletal structures of the two amino acids, glycine and lysine, are given below along with the values of the relevant acid dissociation constants (pKa). NH,* PK, - 10.79 - HạN*CH2CO,¯ S pK¸=2.35 (CH2)4 - H3N*CHCO,- pK,=9,78 lysine (Lys) glycine (Gly) pK, = 9.18 pK, - 2.16 For an aqueous solution of glycine alone, calculate the value of pH at which the ratio of the concentration of neutral glycine zwitterions to the concentration of protonated cation is 102. On your under each of the following conditions. In the blank, provide the total charge of the dipeptide. (Example: If the charge is two plus write the answer simply as 2, if the charge is negative two write the answer as -2). draw the skeletal structure of the dipeptide, Lys-Gly, when it is solvated in an aque us solution i. pH= 1 ii. pH= 12arrow_forwarda)This type of lipid is a complex mixture of esters of long-chain carboxylic acids and long- chain alcohols. b)The number of double bonds present in the metabolic precursor of all prostaglandins. please identify the unknowns. thank you.arrow_forward
- Acetone, CH3–(C=0) –CH3, and urea, NH2–(C=0)–NH2, have similar chemical structures. (a) Compare the possible intermolecular forces for acetone with those for urea. (b) Compare the intermolecular forces between phycocyanin and acetone with those between phycocyanin and water. Briefly explain how acetone disrupts the folding in phycocyanin. (c) Compare the intermolecular forces between phycocyanin and urea with those between phycocyanin and water. Briefly explain how urea disrupts the folding in phycocyanin. (d) Compare your experimental observation on the disruption of phycocyanin folding in the presence of acetone with that in the presence of urea. Briefly explain whether your comparison is consistent with the properties of acetone and urea.arrow_forwardIn each of the following pairs of amino acids, identify which amino acid would be more soluble in water: (a) Ala, Leu; (b) Tyr, Phe; (c) Ser, Ala; (d) Trp, Hisarrow_forwardThe following amino acid is dissolved in solution at pH 7.4. HC H' + CH CH₂ H/ H+ HC a. Which amino acid is this? (all lower case) N- H CH CH₂ b. What is the pKa of its ionizable side chain? (Use the value from the textbook.) c. What is the ratio of the uncharged to the charged form at pH 7.4? (write answer as number with one decimal place, ex 2.5 or 0.2 or 50.0 with an implicit "to 1")arrow_forward
- What structural relationship is indicated by term D glucose.?arrow_forwardA mixture of Alanine (pl 6.02), Glutamic Acid (pl 3.22), Glycine (pl 5.79), Lysine (pl 9.74) 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. Alanine v Second 2. Glutamic Acid v Third 3. Glycine v Fourth 4. Lysine v Fifth 5. Threonine 6. No separationarrow_forward(a) Draw the structure of ninhydrin. (b)Write the complete equation for its reaction with amino acids. (c) What is the substance responsible for the purple colour produced upon reaction of ninhydrin with an amino acid?arrow_forward
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