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Concept explainers
(a)
Interpretation: The interaction present in phenylalanine and leucine 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 arginine 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.
(c)
Interpretation: The interaction present in two cysteine units 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 serine 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.
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Chapter 20 Solutions
EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
- A) Refer to the figure below, Identify and explain the two types of reactions, and describe what are the importance of these reactions to our bodies. Reaction 1 H Monomer Reaction 2 H H OH + H H H₂O H H₂O OH + H H OH OH + H H₂O H₂O OH OH + H OH OH OH OH B) What are the main chemical interactions that determine and maintain the quaternary structure of proteins. Also, what are the conditions that can alter these interactions? [arrow_forwardFor each of the following amino acids: 1) describe what the important functional group of the amino acid side chain is, 2) identify the charge of the side chain, 3) name another component in the structure that the amino acid might interact with, and 4) indicate how the interaction with the component listed in 3) might be occurring (i.e., electrostatic interaction, hydrogen bond, hydrophobic interaction, etc.) a) Asp153 b) Arg166 c) Lys167arrow_forwardΦ 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_forward
- Which of the following statements are False? (i) Parallel b-sheets characteristically distribute hydrophobic side chains on both sides of the sheet, and antiparallel B-sheets are usually arranged with all their hydrophobic residues on one side of the sheet. (ii) Planarity of the peptide bond means that no rotation occurs about the N-Ca bond while rotation is allowed about the C(O)-N and Ca-C(O) bonds. (iii) Silk fibers consist of fibroin proteins consisting of alternating A and G or S residues. (iv) If an aspartic acid residue were present in the interior of a globular protein, it would most likely be deprotonated and thus negatively charged.arrow_forwardDraw the structure and name the following polypeptides: 1. SRAL b. ENIRYTAKarrow_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 structural form of valine that predominates in solution at each of the following ph values: a. ph<pi ; b. pl ; c. ph>pi pk values: pk 1=2.2 ; pk2 = 9.7 Do also for asp (1.88, 9.60, 3.65) and lys (2.88, 8.95, 10.53)arrow_forwardWhat type of interactions is primarily responsible for the creation of the following type of a) Covalent Bonding b) Ionic Interactions c)H-bonding d) Hydrophobic interactions structures? 1. a in the formation of a protein's primary structure 2. C in the formation of an alpha helix 3. d in the formation of a protein's tertiary structure 4. Which of the following polypeptides is capable of forming the most stable alpha helix? a) EEEEEE at pH 7 d) KKKKKK at pH 2 e) PPPPPP at pH 7 b) KKKKKKK at pH 7 (c) EEEEEE at pH 2 5/6. Explain your answer to the previous question. 7. Which of the following is NOT true of a collagen helix or collagen? a) A collagen helix cannot contain prolines. b) A collagen helix has a special amino acid called Hyp c) Collagen is a fibrous protein d) In collagen three helices come together to form a triple helix 8. Which of the following CANNOT make a H-bond. More than one can be circled. a) N-HO-C b) N…H-O-H Ⓒ)C=O....N-C d)C=O....H-O- 9. Which of the following…arrow_forwardClassify the fatty acid with the following structural formula in the ways indicated.a. What is the type designation (SFA, MUFA, or PUFA) for this fatty acid? b. On the basis of carbon chain length and degree of unsaturation, what is the numerical shorthand designation for this fatty acid?c. To which “omega” family of fatty acids does this fatty acid belong? d. What is the “delta” designation for the carbon chain double-bond location for this fatty acid?arrow_forward
- Draw the following: A. a phosphatidylcholine with two oleic acid as the fatty acids B. a phosphatidylethanolamine with two palmitic acid as the fatty acids C. adenine-thymine base pair (show hydrogen bonds via dashed line) D. guanine-cytosine base pair (show hydrogen bonds via dashed line)arrow_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 formula of each of the following: a. Aspartic acid-histidine-tryptophan b. Glycine-cysteine-tyrosine with the charges that exist in cell fluid.arrow_forward
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