6. Proteins contain other amino acids that can compete with cysteine and react with bromoacetamide.Compare the structure of cysteine and serine below. Why can serine react similarly to cysteine? Thinkabout periodic table trends that influence electronic factors.SHIHNHcysteineBrief explanation of why serine can react similarly to cysteine:serineOH

There are four classes of biological macromolecules: protein, nucleic acids, lipids and…

Answered: 6. Proteins contain other amino acids…

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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1. Examine the synthetic glycoprotein, Molecule A, shown below: Protein- OH OH OH OH OH ÓH OH Molecule A OH Draw the structures of the products obtained when Molecule A reacts under the following conditions. Justify your answer. If no reaction occurs, explain why. The monosaccharide rings that have not reacted may be represented by an “R" group. Mechanisms are not required. (а) Ammonium Carbonate, 5 days. (b) Excess Sodium Periodate. (c) 2,3-dinitrophenyl hydrazine under reductive amination conditions. NO2 O2N. „NHNH2 2,3-dinitrophenyl hydrazine
Shown below are three amino acids: H,N-CH-C-o ҫн, H,N-CH-C-o CH, H,N-CH-C-o ČH, Tyrosine Tyr Y Phenylalanine Phe F Alanine Ala A 1. Which amino acid is the least hydrophobic? 2. Which amino acid is most hydrophobic? 3. Which amino acid is intermediate? 4. Explain why (2) is more hydrophobic than (3). 5. Explain why (3) is more hydrophobic than (1).
2) What is glycoside ? In neutral and basic solutions, glycosides do not show mutarotation. However, if the solutions are made acidic, glycosides show mutarotation. Explain why? And write a mutarotation mechanism.
2. Serine is an uncharged, polar amino acid (below and left). Threonine (below and right) is another uncharged, polar amino acid. Illustrate the hydrolysis of a dipeptide that was made from these two amino acids. Be sure to write all involved reactants and products in the structural form like Serine, and as a proper chemical equation; eg. reactant(s) – product(s). Your diagram of the dipeptide must show the N-terminal and C-terminal ends at opposite sides of the dimer molecule, and you need to indicate where the peptide bond is with an arrow/highlighter. H c-C-N OH NH2 CH,-CH -C-COO но CH. он H
29. Amino Acid Chemistry: Using the amino acid chart provided..Ala-Lys-Cys & give the isoelectric point for the tripeptide. Table 23.2 The pK, Values of Amino Acids pk, a-COOH a-NH3* Amino acid side chain Alanine 2.34 9.69 2.17 9.04 12.48 Arginine Asparagine 2.02 8.84 3.86 Aspartic acid Cysteine 2.09 9.82 1.92 10.46 8.35 Glutamic acid 2.19 9.67 4.25 Glutamine 2.17 9.13 Glycine 2.34 9.60 1.82 9.17 6.04 Histidine 2.36 9.68 Isoleucine Leucine 2.36 9.60 2.18 $ 95 10.79 Lysine 2.28 9.21 Methionine 16 9.18 Phenylalanine 1.99 10.60 Proline 2.21 9.15 Serine 2.63 9.10 Threonine 2.38 9.39 Tryptophan Tyrosine 9.11 10.07 2.20 2.32 9.62 Valine O something else! 5.14 O 8.65 something else! 5.81 9.02 9.57
6. Identify the following functional groups AND provide an example of one biomolecule containing that functional group. A B C D E Chemical formula - PO, - COH -OH -COOH -NH₂ Structural formula O -O-P-0° 0= 0- N H -OH C=O OH H H Example: Example: Example: Example: Example: Riomolecules:
Shown below is the structure of a polypeptide with the pK, values of its acidic hydrogens. pK = = 10.1 H OH pK, = 9.2 H. pKa = 2.1 H. N-H pK, = 6.0 pKa = 3.9 1. How many peptide bonds are present in one molecule of the polypeptide? [ Select ] II. Over what pH range would this molecule predominantly exist in a state that has a net charge of zero? [ Select ] ZI
1. An oligosaccharide is a repeating unit of a-D-galactopyranosyl- (a-1- 3)-allopyranoside. Each of the disaccharide unit is linked via B-1-->4 glycosidic bond. Identify and draw the molecular structure. Identify and draw the structure. The oligosaccharide has 10 monosaccharide residue a. Upon the action of alpha-glycosidase, identify and draw all the possible products. b. What is the L-isomer of the Fisher projection of one epimer of D-allopyronoside. Draw the structure. Why is this an epimer of the monosaccharide? c. Is this saccharide a good substrate for glycolysis? Why or why not?
H онн C-C-N -C C-N OH +H20 HH H. H N- C-N-C-C OH OH H. R R The chemical reaction illustrated in the accompanying figure H H C-N-C-C OH N- -C OH R R The chemical reaction illustrated in the accompanying figure O links two monomers to form a polymer separates two phospholipids in a bilayer breaks a peptide bond is a hydrolysis reaction in a polysaccharide A piece of DNA has the following sequence: 5' TCATGG 3'. What would be the sequence of the complementary strand? O 3'AGTACC 5' O S' AGTACC 3 O3 CCATGA 5 O s CCATGA 3 Refer to the accompanying figure. RNA at the beginning of the strands are shaded in lighter color. Identify th leading strand in this figure! O a O b HICIR
arrange the following lipids in order of decreasing polarity: cholesterol, triglyceride, estradiol, fatty acid, phosphatidyl choline
You are studying a novel amino acid. It has an alpha-amino and an alpha-carboxylic group, and an ionizable side chain that carries a carboxylic group. A titration curve is shown below. Net charge a CD f 0 1 2 3 4 5 +1 [Select] 0 [Select] 6 7 pH Choose the letter that corresponds to the following charges on this novel acid. +2 [Select] -0.5 [ [Select] -1 [Select] 8 -2 [Select] I 9 10 11 12 13
Match lipid descriptions in column A with the phospholipid types in column B. H is attached to the phosphate group bound to C3 of glycerol backbone An amino acid is attached to the phosphate group bound to C3 of glycerol backbone A primary ammonium ion is found in its structure A quaternary ammonium ion is found in its structure A. phosphatidylethanolamine B. glycerophospholipid C. phosphatidylcholine D. phosphatidylserine

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