General, Organic, and Biological Chemistry
7th Edition
ISBN: 9781285853918
Author: H. Stephen Stoker
Publisher: Cengage Learning
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Textbook Question
Chapter 20, Problem 20.72EP
Consider the tripeptide leucylvalyltryptophan.
- a. Specify its structure using three-letter symbols for the amino acids.
- b. How many peptide bonds are present within the peptide?
- c. Which of the amino acid residues has the largest R group?
- d. Which of the amino acid residues, if any, has a basic side chain?
Expert Solution & Answer
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Consider the following molecule.
a. Name it.b. Use the three-letter symbols for the amino acids torepresent this molecule.
Two peptide sequences are shown below.Peptide A: N-term – GDL – C-termPeptide B: N-term – GTL – C-terma. Draw each peptide at physiological pH. Circle each ionizable functional group in your drawing.b. Briefly explain why changing aspartate to threonine changes the number of ionizable functionalgroups in the peptide chain.c. Briefly explain why the functional group found in aspartate’s side chain is ionizable but the functionalgroup found in threonine’s side chain is not.
Suppose that the sequence is part of a larger globular protein.
Consider the probable location, either on the external surface
or the interior of the protein, of each of the amino
acid residues.
The table gives the hydropathy index values for selected
amino acids in the peptide.
Amino acid
Hydropathy index
alanine
1.8
isoleucine
4.5
threonine
-0.7
glutamine
-3.5
lysine
-3.9
aspartate
-3.5
Chapter 20 Solutions
General, Organic, and Biological Chemistry
Ch. 20.1 - Prob. 1QQCh. 20.1 - Proteins are naturally occurring unbranched...Ch. 20.2 - Prob. 1QQCh. 20.2 - How do the various standard amino acids differ...Ch. 20.2 - The number of carboxyl groups and amino groups...Ch. 20.2 - How many different subclassifications are there...Ch. 20.2 - Which of the following statements concerning...Ch. 20.3 - Prob. 1QQCh. 20.3 - Proteins from plant sources are a. always complete...Ch. 20.3 - Prob. 3QQ
Ch. 20.4 - Prob. 1QQCh. 20.4 - Which of the following groups is positioned at the...Ch. 20.4 - Which of the following statements concerning...Ch. 20.5 - Which of the standard amino acids exist as...Ch. 20.5 - Which of the following is the zwitterion ion...Ch. 20.5 - Which of the following is the structural form for...Ch. 20.6 - Prob. 1QQCh. 20.6 - Prob. 2QQCh. 20.7 - The joining together of two amino acids to form a...Ch. 20.7 - The number of peptide bonds present in a...Ch. 20.7 - Which of the following statements concerning the...Ch. 20.7 - Prob. 4QQCh. 20.7 - How many isomeric tripeptides can be formed from...Ch. 20.8 - The two best-known peptide hormones present in the...Ch. 20.8 - Which of the following peptides is an important...Ch. 20.9 - The term protein is generally reserved for...Ch. 20.9 - Prob. 2QQCh. 20.9 - Which of the following is not a distinguishing...Ch. 20.10 - Specifying the primary structure of a protein...Ch. 20.10 - Prob. 2QQCh. 20.10 - Prob. 3QQCh. 20.11 - Prob. 1QQCh. 20.11 - Prob. 2QQCh. 20.11 - Prob. 3QQCh. 20.12 - Prob. 1QQCh. 20.12 - Hydrophobic interactions associated with protein...Ch. 20.12 - R group interactions between which of the...Ch. 20.13 - Prob. 1QQCh. 20.13 - Which of the following types of interactions does...Ch. 20.14 - The complete hydrolysis of a protein produces a...Ch. 20.14 - Which of the following statements concerning...Ch. 20.15 - Which of the following levels of protein structure...Ch. 20.15 - Which of the following does not involve protein...Ch. 20.15 - Prob. 3QQCh. 20.16 - Prob. 1QQCh. 20.16 - Prob. 2QQCh. 20.16 - Prob. 3QQCh. 20.16 - In which of the following pairs of proteins are...Ch. 20.17 - Insulin and human growth hormone are examples of...Ch. 20.17 - Myoglobin and transferrin are examples of a....Ch. 20.17 - Prob. 3QQCh. 20.18 - Prob. 1QQCh. 20.18 - Prob. 2QQCh. 20.18 - Prob. 3QQCh. 20.19 - Prob. 1QQCh. 20.19 - Which of the following types of plasma...Ch. 20.19 - Prob. 3QQCh. 20 - Prob. 20.1EPCh. 20 - What element is always present in proteins that is...Ch. 20 - What percent of a cells overall mass is accounted...Ch. 20 - Approximately how many different proteins are...Ch. 20 - What is signified when an amino acid is designated...Ch. 20 - What functional groups are present in all -amino...Ch. 20 - Indicate whether or not each of the following...Ch. 20 - Indicate whether or not each of the following...Ch. 20 - How many carbon atoms are present in the R group...Ch. 20 - How many carbon atoms are present in the R group...Ch. 20 - With the help of Table 20-1, determine the name...Ch. 20 - With the help of Table 20-1, determine the name...Ch. 20 - With the help of Table 20-1, classify each of the...Ch. 20 - With the help of Table 20-1, classify each of the...Ch. 20 - Prob. 20.15EPCh. 20 - With the help of Table 20-1, classify each of the...Ch. 20 - Prob. 20.17EPCh. 20 - Prob. 20.18EPCh. 20 - Prob. 20.19EPCh. 20 - Prob. 20.20EPCh. 20 - Prob. 20.21EPCh. 20 - How many amino groups and how many carboxyl groups...Ch. 20 - Prob. 20.23EPCh. 20 - Which two of the standard amino acids are...Ch. 20 - Prob. 20.25EPCh. 20 - Prob. 20.26EPCh. 20 - Prob. 20.27EPCh. 20 - Prob. 20.28EPCh. 20 - Prob. 20.29EPCh. 20 - Prob. 20.30EPCh. 20 - Indicate whether or not the designation...Ch. 20 - Indicate whether or not the designation...Ch. 20 - Prob. 20.33EPCh. 20 - Prob. 20.34EPCh. 20 - To which family of mirror-image isomers do nearly...Ch. 20 - In what way is the structure of glycine different...Ch. 20 - Draw Fischer projection formulas for the following...Ch. 20 - Draw Fischer projection formulas for the following...Ch. 20 - Answer the following questions about the amino...Ch. 20 - Answer the following questions about the amino...Ch. 20 - At room temperature, amino acids are solids with...Ch. 20 - At room temperature, most amino acids are not very...Ch. 20 - Prob. 20.43EPCh. 20 - Draw the zwitterion structure for each of the...Ch. 20 - Draw the structure of serine at each of the...Ch. 20 - Prob. 20.46EPCh. 20 - Prob. 20.47EPCh. 20 - Most amino acids have isoelectric points between...Ch. 20 - Glutamic acid exists in two low-pH forms instead...Ch. 20 - Arginine exists in two high-pH forms instead of...Ch. 20 - In a low-pH aqueous solution, indicate whether...Ch. 20 - Prob. 20.52EPCh. 20 - When two cysteine molecules dimerize, what happens...Ch. 20 - What chemical reaction involving the cysteine...Ch. 20 - What two functional groups are involved in the...Ch. 20 - Write a generalized structural representation for...Ch. 20 - For the tripeptide GlyAlaCys a. What amino acid is...Ch. 20 - For the tripeptide SerValMet a. What amino acid is...Ch. 20 - Prob. 20.59EPCh. 20 - Prob. 20.60EPCh. 20 - Draw a complete condensed structural...Ch. 20 - Draw a complete condensed structural...Ch. 20 - With the help of Table 20-1, identify the amino...Ch. 20 - With the help of Table 20-1, identify the amino...Ch. 20 - With the help of Table 20-1, assign an IUPAC name...Ch. 20 - With the help of Table 20-1, assign an IUPAC name...Ch. 20 - Prob. 20.67EPCh. 20 - Prob. 20.68EPCh. 20 - For the tripeptide AlaValGly which amino acid...Ch. 20 - For the tripeptide SerArgIle which amino acid...Ch. 20 - Consider the tripeptide tyrosylleucylisoleucine....Ch. 20 - Consider the tripeptide leucylvalyltryptophan. a....Ch. 20 - Explain why the notations SerCys and CysSer...Ch. 20 - Explain why the notations AlaGlyValAla and...Ch. 20 - Prob. 20.75EPCh. 20 - There are a total of six different amino acid...Ch. 20 - Compare the structures of the protein hormones...Ch. 20 - Compare the protein hormones oxytocin and...Ch. 20 - Compare the binding-site locations in the brain...Ch. 20 - Compare the structures of the peptide...Ch. 20 - Prob. 20.81EPCh. 20 - Prob. 20.82EPCh. 20 - What is the major difference between a monomeric...Ch. 20 - What is the major difference between a simple...Ch. 20 - Prob. 20.85EPCh. 20 - Prob. 20.86EPCh. 20 - Prob. 20.87EPCh. 20 - Two proteins with the same amino acid composition...Ch. 20 - How many different primary structures are possible...Ch. 20 - How many different primary structures are possible...Ch. 20 - How many different primary structures are possible...Ch. 20 - How many different primary structures are possible...Ch. 20 - Prob. 20.93EPCh. 20 - Draw a segment of the backbone of a protein that...Ch. 20 - Prob. 20.95EPCh. 20 - In a pleated sheet secondary structure for a...Ch. 20 - Indicate whether each of the following statements...Ch. 20 - Indicate whether each of the following statements...Ch. 20 - Prob. 20.99EPCh. 20 - Prob. 20.100EPCh. 20 - State the four types of attractive forces that...Ch. 20 - Prob. 20.102EPCh. 20 - Prob. 20.103EPCh. 20 - Prob. 20.104EPCh. 20 - Prob. 20.105EPCh. 20 - Prob. 20.106EPCh. 20 - Prob. 20.107EPCh. 20 - Prob. 20.108EPCh. 20 - Prob. 20.109EPCh. 20 - Not all proteins have quaternary structure....Ch. 20 - Prob. 20.111EPCh. 20 - Prob. 20.112EPCh. 20 - Prob. 20.113EPCh. 20 - Prob. 20.114EPCh. 20 - Prob. 20.115EPCh. 20 - Prob. 20.116EPCh. 20 - Prob. 20.117EPCh. 20 - Prob. 20.118EPCh. 20 - Identify the primary structure of a hexapeptide...Ch. 20 - Identify the primary structure of a hexapeptide...Ch. 20 - Draw structural formulas for the products obtained...Ch. 20 - Prob. 20.122EPCh. 20 - Which structural levels of a protein are affected...Ch. 20 - Prob. 20.124EPCh. 20 - In what way is the protein in a cooked egg the...Ch. 20 - Why is cooked protein more easily digested than...Ch. 20 - Indicate whether or not each of the following...Ch. 20 - Prob. 20.128EPCh. 20 - Prob. 20.129EPCh. 20 - Contrast fibrous and globular proteins in terms of...Ch. 20 - Classify each of the following proteins as a...Ch. 20 - What is the major biochemical function of each of...Ch. 20 - Prob. 20.133EPCh. 20 - Prob. 20.134EPCh. 20 - Prob. 20.135EPCh. 20 - Prob. 20.136EPCh. 20 - Prob. 20.137EPCh. 20 - Where are the carbohydrate units located in...Ch. 20 - Prob. 20.139EPCh. 20 - Prob. 20.140EPCh. 20 - Prob. 20.141EPCh. 20 - Prob. 20.142EPCh. 20 - Prob. 20.143EPCh. 20 - Describe the process by which blood...Ch. 20 - Prob. 20.145EPCh. 20 - Prob. 20.146EPCh. 20 - Prob. 20.147EPCh. 20 - Prob. 20.148EPCh. 20 - Prob. 20.149EPCh. 20 - Prob. 20.150EPCh. 20 - Prob. 20.151EPCh. 20 - Prob. 20.152EP
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- Using the amino acid phenylalanine, draw and specify the nature of each following tertiary structure interactions between:a. two cysteinesb. arginine and glutamic acidc. isoleucine and tyrosinearrow_forwarda. Draw the peptide chain (indicate if it is solid or hatched wedges) for the following: Glycine-(L)-Arginine-(D)-Proline-(L)-Glutamic Acid b. Compute for the isoelectric point. Show solution.arrow_forwardConsider the following peptide: alanyl-glutamyl-lysyl-cysteyl-asparagine. 1- Write the semi-developed formula of this peptide at pH = 1. Indicate the N- terminal and C-terminal ends of the peptide. Indicate the carbones a. 2- This peptide comprises 5 ionisable groups whose pKa values are, respectively: 2 ; 4.3 ; 8.3 ; 9.7 ; 10.5. Attribute a pKa value to each ionisable group. Justify your answer answer (using the Table, p. 8 when necessary).arrow_forward
- Draw the L enantiomer in a Fischer projection for each amino acid; identify the amino acid as neutral, acidic, or basic. Give the three-letter sign [3], and the one-letter symbol [4].arginine a. arginine b. arginine c. a. glutamic acid b. glutamic acid c. glutamic acidtyrosine b. valine c. argininearrow_forwardExplain why amino acid can increase blood glucose. Write the structure of each of the following peptide at pH7 and identify how many peptide bond in each number. Alanyl-phenylalanine- aspartate- cysteine Threonyl- Isoleucyl-methionyl- leucine Lysyl-alanine -Phenylalanyl-tyrosyl- serinearrow_forwardConsider the peptide with amino acid sequence NICE. a. Write the full name and the three-letter abbreviations of the amino acids in the peptide. b. Calculate the net charge of the peptide at pH 7.0. Show you work in a table. c. Calculate the pI of the peptide. Show you work in a table.arrow_forward
- Write the structure, identify the groups and describe the chemical properties of these amino acids. A. alanine B. Serine C. Leucine D. Phenylalanine E. Tryptophanarrow_forwardFor the following pentapeptides: Ser-Glu-Gly-His-Ala and Gly-His-Ala-Glu-Ser A. Compute their isoelectric pH (pI). Show full solution. Use standard pKa values. B. Do these peptides with the same amino acid composition have different net charges at pH 7.0? Explain briefly. C. Would you expect the titration curves of the two peptides to differ? Why or Why not?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
- a. A tetrapeptide is abbreviated as PSQE. Write the name of the amino acid at the N-terminal end. b. A tetrapeptide is abbreviated as FRWL. Write the name of the amino acid at the C-terminal end.arrow_forwardConsider the following situation; Fresh pineapple contains the enzyme bromelain that hydrolyzes peptide bonds in proteins. a. The directions in making a gelatin (protein) dessert say not to add fresh pineapple. However, canned pineapple where pineapple is heated to high temperatures can be added. Why? b. Fresh pineapple is used in a marinade to tenderize tough meat. Why? c. What structural level of a protein does the bromelain enzyme destroy?arrow_forwardCalculate the isoelectric point for each amino acid.a. asparagine: pKa (COOH) = 2.02; pKa (α-NH3+) = 8.80b. methionine: pKa (COOH) = 2.28; pKa (α-NH3+) = 9.21arrow_forward
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