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Concept explainers
(a)
Interpretation: The interaction present in lysine and aspartic acid has to be stated.
Concept introduction: The four types of attractive forces that give rise to tertiary proteins are: covalent disulphide bonds, electrostatic attractions, hydrogen bonds and hydrophobic attractions.
(b)
Interpretation: The interaction present in threonine and tyrosine has to be stated.
Concept introduction: The four types of attractive forces that give rise to tertiary proteins are: covalent disulphide bonds, electrostatic attractions, hydrogen bonds and hydrophobic attractions.
(c)
Interpretation: The interaction present alanine and valine has to be stated.
Concept introduction: The four types of attractive forces that give rise to tertiary proteins are: covalent disulphide bonds, electrostatic attractions, hydrogen bonds and hydrophobic attractions.
(d)
Interpretation: The interaction present in leucine and isoleucine has to be stated.
Concept introduction: The four types of attractive forces that give rise to tertiary proteins are: covalent disulphide bonds, electrostatic attractions, hydrogen bonds and hydrophobic attractions.
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Chapter 20 Solutions
EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
- Φ and ψ in the Ramachandran plot (below) are: a) Rotational angles around the bond between the α-carbon and N-H (Φ) and C=O (ψ). b) Amino acid solubility in octanol (Φ) and water (ψ). c) Hydrogen bond angles in α-helices (Φ) and β-sheets (ψ). d) Amino acid solubility in water (Φ) and octanol (ψ).arrow_forwardb) It's said that secondary structures form because of intra- and intermolecular hydrogen bonding involving the peptide bond. Describe what is going on to further stabilize secondary structure through these interactions.arrow_forwardDraw the structural formulas of the following peptides, andshow which bond would be cleaved by chymotrypsin.a. trp-val-glyb. phe-ala-proarrow_forward
- Draw the following amino acids described below include all hydrogens in the structure. 1)amino acid Proline at pH2.0. 2) amino acid glycine at pH 3.0. 3) amino acid with a Methionine at pH 7.0. 4) the amino acid Histidine at pH5.0.arrow_forwardDescribe the forces that are involved in the tertiary structure of a protein and give an example of each force listed.arrow_forwardFor each amino acid: [1] draw the L enantiomer in a Fischer projection; [2] classify the amino acid as neutral, acidic, or basic; [3] give the three-letter symbol; [4] give the one-letter symbol. a. arginine c. glutamic acid b. tyrosine d. valinearrow_forward
- Identify the following types of biomolecules and label and identify the functional groupsarrow_forwardIn x-ray studies of crystalline peptides, Linus Pauling and Robert Corey found that the C—N bond in the peptide link is intermediate in length(1.32 Å) between a typical C—N single bond (1.49 Å) and a C=N double bond (1.27 Å). They also found that the peptide bond is planar (all four atoms attached to the C—N group are located in the same plane) and that the two α-carbon atoms attached to the C—N are always trans to each other (on opposite sides of the peptide bond).(a) What does the length of the C—N bond in the peptide linkage indicate about its strength and its bond order (i.e., whether it is single, double, or triple)?(b) What do the observations of Pauling and Corey tell us about the ease of rotation about the C—N peptide bond?arrow_forwardDraw the following amino acids interactions: 1. H-bond - between -0H of Serine amino acid and C=0 backbone of glutamic acid. 2. Ionic bond- between ionized aspartic and asparagine amino acids. 3. Disulfide interaction between 2 molecules of Cysteine amino acids. 4. Hydrophobic interaction between Alanine and Leucine R-groups.arrow_forward
- Which of the following is incorrect? (₁) a. A heterodimer is composed by two identical polypeptide chains b. The polypeptide chains in a multimeric protein are called subunits A homotrimer can be represented with the Greek letter alpha with a sub-index 3 d. Monomeric proteins do not have quaternary structure c.arrow_forwardMake use of the table below in answering the questions asked: Amino acid pK₁ pK₂ pK, Isoleucine 2.32 9.76 Leucine 2.32 9.74 Lysine 2.16 9.06 10.54 Tyrosine 2.20 9.21 10.46 1. Kindly draw manually the structure of tripeptic ILY at pH 7.00 2. Kindly draw manually the most protonated structure of tripeptide ILYarrow_forwardUse the pka values, calculate the isoelectric point (pl) of the following amino acids. a) Leucine b) Arginine c) Aspartic acid d) Glutamic acid Amino Acid Alanine Arginine Asparagine Aspartic acid Cysteine Glutamic acid Glutamine Glycine Histidine Isoleucine Leucine Lysine Methionine Phenylalanine Proline Serine Threonine Tryptophan Tyrosine Valine pk, of a-COOH 2.35 2.01 2.02 2.10 2.05 2.10 2.17 2.35 1.77 2.32 2.33 2.18 2.28 2.58 2.00 2.21 2.09 2.38 2.20 2.29 pk of a-NH,* 9.87 9.04 8.80 9.82 10.25 9.47 9.13 9.78 9.18 9.76 9.74 8.95 9.21 9.24 10.60 9.15 9.10 9.39 9.11 9.72 pk of Side Chain 12.48 - 3.86 8.00 4.07 6.10 - 10.53 II 10.07 -arrow_forward
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