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EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
7th Edition
ISBN: 8220100853180
Author: STOKER
Publisher: CENGAGE L
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Question
Chapter 20.10, Problem 2QQ
Interpretation Introduction
Interpretation: When specifying the primary structure of a protein, the location of first amino acid has to be predicted.
Concept introduction: Every protein molecule has its own unique sequence of amino acids. The primary protein structure represents the order in which amino acids are linked. It involves the order of attachment of the amino acids to each other through peptide bonds.
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Students have asked these similar questions
Which of the following statements are correct about the native state of a protein (select all that apply)?
A.
Polar sidechains commonly interact with water
B.
Hydrophobic amino acids tend to be on surface of protein
C.
The sidechains of polar amino acids are most commonly found in the central core of a protein
D.
Formation of an alpha-helix is primarily driven by hydrogen bonds between the protein main chain, not sidechains.
E.
Secondary structure is largely driven by hydrophobic interactions
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.
Which of these amino acids is a polar, uncharged amino acid? (Select all that apply, if necessary.)
A.
B.
D.
E.
CHLO
H₂N-CH-C
CH₂
CH₂
CH₂
NH
C=NH2
NH₂
amino acid A
amino acid C
amino acid D
amino acid B
amino acid E
H₂N-CH-C
CH₂
_i_g
C.
H₂N-CH-C-
CH2₂
I
CH₂
=0
NH₂
H₂N-CH-
CH₂
CH-CH3
CH3
H₂ND
H₂N-CH-
|
CH₂
Ï
OH
Chapter 20 Solutions
EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
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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- Define the following terms:a. polypeptideb. peptidec. proteind. peptide bonde. standard amino acidsarrow_forwardDescribe the levels of structure of a protein and tell how they would be affected by: a. Hydrolysis with 6M HCl (breaks peptide bond)b. Heating with mercaptoethanol (breaks hydrogen bonds)arrow_forwardWhich of the following might cause the denaturation of a protein? Select all that apply. A. Highly acidic conditions B. Highly basic conditions C. High concentrations of salt D. High heatarrow_forward
- Imagine the main chain of a protein bends back on itself, so that two amino acid residues R, and R, come close to each other. In the table below are four possibilities for what R, and R, might be. In each case, decide whether a specific interaction could form between the residues. If a specific interaction could form, give the name of the interaction. R1 R2 specific interaction? name of specific interaction O yes serine tyrosine O no О yes valine threonine O no O yes threonine glutamine O no О yes cysteine cysteine noarrow_forward+H₂N-CH-COO™ T CH₂ I CH₂ 1 CH₂ I +H₂N-CH₂ A. O amino acid C amino acid D O amino acid E amino acid B +H₂N-CH-COO™ I CH₂ I CH₂ 1 O amino acid A C=0 B. If the pH decreases enough, this amino acid will become protonated and could contribute to the denaturation of the protein. +H₂N-CH-COO™ 1 CH₂ I OH C. +H₂N-CH-COO™ CH H₂C CH3 D.arrow_forwardGiven below are sequences of amino acids present in an oligo-peptide chain. Count the overall charge of each assigned peptide and write it in your answer. Along with it also mention that toward which electrode (cathode or anode) will the peptide move? Please remember that cathode is a negativeelectrode and anode is a positive electrode. Ile-Lys-Arg-Trp-Lys-Asn-Glu-His-Pro-Asp-Ala-Tyr-Phe-Glu-Met-Phe-Gly-Valarrow_forward
- When the amino acid sequence of Hb and Mb is compared, some of them are found to be the same (invariant). The reason that these residues are found in both proteins in the same positions is: (choose all the correct answers) a.They are residues found on the carboxyl terminal side of Mb and Hb that help their solubility. b.They are part of the surface of Hb and Mb that help their solubility. c.They are crucial residues for the function of these proteins. d.They are residues that have been conserved evolutionarily.arrow_forwardA protease is an enzyme that catalyzes the hydrolysis of the peptide bonds of target proteins. How might a protease bind a target protein so that its main chain becomes fully extended in the vicinity of the vulnerable peptide bond?arrow_forwarda. How many peptide bonds are there? b. How many amino acid residues are there? c. In exact order, identify the name of the amino acids in the peptide chain. d. Give the full name of this peptide. e. Give the 3-letter abbreviation and 1-letter abbreviation. f. Calculate the pI of this peptide.arrow_forward
- This image shows the tertiary structure of a protein segment. Tertiary structure results from different interactions, or forces, between groups. Move the example of each force to the appropriate description on the protein. Then, identify the major force controlling tertiary structure. (Need help) It says I'm wrong.arrow_forwardUsing one of the lower level structures, explain how the protein’s effects one of the higher level of structure (primary influencing tertiary, secondary influencing tertiary, tertiary influences on quaternary, ect.)arrow_forwardWhich of the following describes the most likely outcome of a mutation that causes a sin- gle amino acid to be removed from a protein subunit? A It will affect the primary, secondary, and tertiary structures of the protein. B с D It will affect the secondary and tertiary structures of the protein but not the primary structure. There will be no observable effect on the structure of the protein. It will change the primary structure of the protein without affecting other structures in the protein.arrow_forward
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