9. Titration of valine by a strong base, for example NaOH, reveals two pK's. The titration reaction occurring atpK2 (pK2 = 9.62) is:a) —СООН + Он -> —соо" + Н20.b) -COOH + -NH2 -> -COO" +-NH2*.c) -co0 +-NH2* ->-COOH +–NH2.d) –NH3* + OH" -> –NH2 + H2O.e) –NH2 + OH -> –NH + H2O.10.In a highly basic solution, pH = 13, the dominant form of glycine is:а) NH2—CH2—СООН.b) NH2-CH2-coO".c) NH2-CH3*-coo.d) NH3*-CH2-COOH.e) NH3*-CH2-coo".

Answer 9 - option D) -NH3+ + OH → ¬NH₂ + H₂0 Explanation: Valine has two acid-base groups: the…

Answered: 9. Titration of valine by a strong…

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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Titration of alanine by a strong base, for example NaOH, reveals two pk's. Which is the titration reaction occurring at pK1 (pK1 = %3D 2.34)? O-NH2 + COH →-NH + H2O O-COOH + OH →-CO + H20 -COOH + -NH2 → -COO" + -NH2+ -CoO +-NH2* → -COOH +-NH2 O -NH3* + OH →-NH2 + H2O
Select the term in column B which best matches the description in column A. There are more terms then needed. Column A Column B 1. The pentose sugar found in DNA. a) Cis fatty acid b) Trans fatty acid c) Coenzyme d) Cofacipr 2. Commonly referred to as "insoluble fiber". 3. Considered to be an amphipathic molecule. 4. A molecule with the formula C18H3602 is probably a e) Phospholipid 5. Bond created during the formation of the primary structure of a protein. ) Glycogen 6. A non-protein organic molecule needed for proper enzyme functioning. g) Cellulose 7. Pyrimidine base found only in RNA. h) Galactose i) Fructose 8. Increasing the number of these molecules in the cell membrane would increase the permeability of the cell membrane. i) Thymine k) Uracil 9. Bond which connects nucleotide monomers together. 1) Fatty acid m) Disaccharide n) Peptide bond o) A-Helix p) B-Pleated Sheet q) Ribose r) Deoxyribose 10.
An oligopeptide has the following amino acid sequence: NH2-Ala-Glu–Leu–Trp–Tyr-Ser–Gly–Lys–Leu-Ala–Arg-Ala-Phe-Ile-Pro–Gly-COOH a) Estimate the net electric charge of the molecule at pH 8.0 and pH 11.0. b) If the above peptide is passed through a cation exchange chromatographic column (that is, the matrix of the column has negative charges) stabilized at pH 8.0, would you expect it to be retained on the column? c) Indicates the number of fragments, and the sequence of each of them, that would be obtained when treating the peptide in question with: i) trypsin, ii) chymotrypsin.
8) The amino acid Cysteine has this structure and pka's: SH (8.00) (10.25) H3N+ CH₂ -COOH (2.05) a) Sketch the titration curve of Cysteine (originally at pH = 0) vs. NaOH. b) At what pH is Cysteine most water soluble?
. The following diagram shows the biosynthesis of B12 coenzymes, starting with the vitamin. DMB is dimethylbenzimidazole. (a) What one additional substrate or cofactor is required by enzyme B? (b) Genetic deficiency in animals of enzyme C would result in exces- sive urinary excretion of what compound?
A) Upon entering the body, CH3H9+ reacts with cysteine to form a molecule that is able to pass through the blood brain barrier (BBB). Draw the structure of this molecule and purpose why it is able to pass through the BBB (Hint: think about another amino acid). B) The adduct formed in part A is very labile. On encountering selenocysteine, it can permanently inhibit it. Propose how the adduct from Part A inhibits selenocysteine and explain your answer.
Imagine that a mutation has been discovered in the HBA1 gene, where amino acid residue # 1 in the alpha subunit is changed from valine to lysine. The structure of these two amino acids is shown below. How would this mutation affect the mobility of HbA in the gel?a) HbA with this mutation would have the same mobility as normal HbAb) HbA with this mutation would have the same mobility as HbSc) HbA with this mutation would have a faster mobility than normal HbA O d) HbA with this mutation would have a mobility somewhere in between HbS and normal HbA
1. The R group of the amino acid lysine is: -CH2-CH2-CH2-CH2-NH2. Draw the structure of lysine, including the sites of ionization, under the following conditions: 16 NI a) strongly acidic solution; b) neutral solution; c) strongly basic solution Drifed them ard What are the results of the following test on lysine? c) nitroprusside a) ninhydrin; b) biuret;
A) Draw L-histidine. Label all ionizable groups with the appropriate pKa.
In the deoxy state of HB, which of the following does not occur? a) An inter-chain salt bridge between Histidine 146 and Lys 40 b) An intra-chain salt bridge between Val 98 and Tyr 145. c) An intra-chain salt bridge between Histidine 146 and Aspartate 94 side chains d) A peptide bond between Tyr 145 and His 146.
25) Below are two amino acids: cysteine and histidine. a) Draw the reaction mechanism of a dehydration synthesis reaction between cysteine and histidine below: HS H Product 1 OH ox HN H b) Draw two different products of the dehydration synthesis reaction from part a). Prove that these are two different products by labelling the N and C termini, peptide bond, and R-groups of each product. Product 2 OH
25) Below are two amino acids: cysteine and histidine. a) Draw the reaction mechanism of a dehydration synthesis reaction between cysteine and histidine below: HS H Product 1 N OH HN H b) Draw two different products of the dehydration synthesis reaction from part a). Prove that these are two different products by labelling the N and C termini, peptide bond, and R-groups of each product. Product 2 OH

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