Biology
12th Edition
ISBN: 9780134813448
Author: Audesirk, Teresa, Gerald, Byers, Bruce E.
Publisher: Pearson,
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Textbook Question
Chapter 3.4, Problem 1CSC
Infectious prions such as those that cause mad cow disease are abnormally folded versions of a protein that is found throughout the body. The secondary structure of the normal prion protein is primarily helical. Infectious prions, however, fold into pleated sheets. The pleated sheets are so stable they are unaffected by the enzymes that break down normal prion protein. As a result, infectious prions accumulate destructively in the brain.
Helices and pleated sheets are the two major secondary structures of proteins. What do protein tertiary and Quaternary structures look like?
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It is often the case that a helices are positioned in a protein such that one side faces the interior of the protein and the other, the surface of the protein. These are
said to be amphiphilic helices because they face different environments. Using a helical wheel projection (shown below), which of the peptide(s) below might form
an amphiphilic helix?
8
15
1
12
4
11
16
18
9
7
14
13
10
17
O SLIKSVIEMVDEWFRTFL
O FLIRVLRKVFRVLTRILS
O RLFRSRVLKIAVIRFLLI
What general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)?
Only one answer is correct.
the surface consists of hydrophilic alpha-helix.
the surface is highly modified by post-translational modification.
the surface is permanently bound by chaperones.
the surface is unstructured.
the surface, or part of it, is self-complementary.
How many amino acids are present on the helix to the right? Any
partially drawn amino acids count as one whole amino acid
Circle one peptide bond and box one R group on the figure to the
right
Describe how a lack of Vitamin C in the diet will affect the overall
structure of collagen.
Figure 6-7
Illustration, Irving Gels. Image from the Irving Geis Collection/Howard Hughes
Medical Institute. Rights owned by HHMI. Reproduction by permission only.
Drotoinc
Chapter 3 Solutions
Biology
Ch. 3.1 - which of these is/are polar molecules? (you may...Ch. 3.1 - define organic molecules and explain why carbon is...Ch. 3.1 - explain why functional groups are important in...Ch. 3.1 - name and describe the properties of seven...Ch. 3.2 - define organic molecules and explain why carbon is...Ch. 3.3 - Describe hydrolysis of this molecule.Ch. 3.3 - describe the major types of carbohydrates?Ch. 3.3 - provide examples of each type of carbohydrate and...Ch. 3.4 - Look up the rest of the amino acids and. based on...Ch. 3.4 - Infectious prions such as those that cause mad cow...
Ch. 3.4 - Why do many proteins, when heated excessively....Ch. 3.4 - Why a Perm Is (Temporarily) Permanent?Ch. 3.4 - describe protein subunits and how proteins are...Ch. 3.4 - explain the four levels of protein structure and...Ch. 3.4 - list several functions of proteins and provide...Ch. 3.4 - Prob. 4CYLCh. 3.5 - describe the general structure of nucleotides?Ch. 3.5 - list three different functions of nucleotides?Ch. 3.5 - explain how nucleic acids are synthesized?Ch. 3.5 - give two examples of nucleic acids and their...Ch. 3.5 - Puzzling Proteins All cells use DNA as a blueprint...Ch. 3.6 - What kind of reaction breaks this molecule apart?Ch. 3.6 - An obese 55-year-old woman consults her physician...Ch. 3.6 - Why are steroid hormones able to diffuse through...Ch. 3.6 - compare and contrast the structure and synthesis...Ch. 3.6 - describe the functions of fats, oils, and waxes?Ch. 3.6 - Prob. 3CYLCh. 3.6 - Prob. 1CTCh. 3 - Polar molecules a. dissolve in lipids. b. are...Ch. 3 - Prob. 2MCCh. 3 - Prob. 3MCCh. 3 - Which of the following is not composed of...Ch. 3 - Prob. 5MCCh. 3 - In organic molecules made of chains of subunits,...Ch. 3 - Prob. 2FIBCh. 3 - Prob. 3FIBCh. 3 - Prob. 4FIBCh. 3 - Fill in the following with the appropriate type of...Ch. 3 - Prob. 1RQCh. 3 - List the four principal classes of biological...Ch. 3 - Prob. 3RQCh. 3 - Prob. 4RQCh. 3 - Prob. 5RQCh. 3 - Describe the synthesis of a protein from amino...Ch. 3 - Where in nature do we find cellulose? Where do we...Ch. 3 - Based on their structure, sketch and explain how...Ch. 3 - Prob. 2ACCh. 3 - Prob. 3AC
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- What is Protein folding? Give at least 3 diseases that results from protein misfolding. Explain each. Can you give me a brief explanation about this question? Not less than 3 sentences.arrow_forwardA particular DNA sequence encodes for MRNA that then encodes for the amino acid glutamate in a protein. A mutation occurs in the DNA that changes the MRNA codon for the glutamate into a different codon. Which change would cause the least disruption to the structure of the protein? Hint: Think about the nature of the various R groups (side-chains) of the amino acids, and how intermolecular forces/interactions govern the way a protein folds into its three-dimensional structure. The codon for the glutamate is changed into a stop codon. The codon for the glutamate is changed into the codon for aspartate. O The codon for the glutamate is changed into the codon for phenylalanine. O The codon for the glutamate is changed into the codon for serine.arrow_forwardConsider the following protein sequence as an α helix: Leu-Lys-Arg-Ile-Val-Asp-Ile-Leu-Ser-Arg-Leu-Phe-Lys-Val. how many turns does this helix make?arrow_forward
- Two proteins are discovered, and both are shown to have a potential in treating fatty liver disease. The structural differences of the proteins require them to be delivered using spherical nanoparticles made of different polymers. The scientists are trying to decide which protein will be more efficient to use in applications where a faster drug release is more favorable. Protein 1 is loaded into spherical nanoparticles made of polymer 1 which has R=100 nm at a concentration of 50 nM. Protein 2 is loaded into spherical nanoparticles made of polymer 2 which has R=250 nm, at a concentration of 50 nM. The partition coefficient of polymer 1 is 0.01 and is known to be half of partition coefficient of polymer 2. The diffusion coefficient of protein 1 in polymer 1 is 2x10-6 cm2/s, and diffusion coefficient of protein 2 in polymer 2 is 3.4x10-6 cm2/s. Determine which treatment will be selected for treatment of fatty liver disease.arrow_forwardConsider the following peptide to answer the questions below: A M A K K E S H I F T A I D E What is the total charge of this peptide at pH = 5? What is the N terminal amino acid (full name)? C terminal amino acid? How many fragments would result if this peptide underwent proteolytic cleavage with V-8 protease and what are these fragments (list them)? Would this peptide be a candidate to form an alpha helix? Why or why notarrow_forwardPro-CHEMBIO peptide is a large peptide sequence with three disulfide bonds (indicated by the lines between cysteine residues). CHEMBIO Protease cleaves amide bonds between two basic amino acid residues to give the final peptide that is active in the body. The products of this protease reaction are: 1. Two chains that make up active CHEMBIO peptide, which contain the N- and C-terminus sections of the original Pro-CHEMBIO molecule 2. A separate inactive peptide What if instead of CHEMBIO Protease, this peptide was cleaved by trypsin? Indicate the cleavage locations on the structure below. asaparrow_forward
- Assume that the 3 polypeptide strands shown below form a parallel B-sheet. Select amino acids AA1, AA2, and AA3 so that the parallel B-sheet is amphipathic and remains stable. Glu-lle-Asn-AA1-Cys-Val Ser-AA2-GIn-Leu-Lys-Phe Lys-Met-Cys-Leu-AA3-Val O AA1 = Pro, AA2 = Leu, AA3 = lle O AA1 = Val, AA2 = Leu, AA3 = Asn O AA1 = Ala, AA2 = Gly, AA3 = Leu AA1 = Phe, AA2 = Arg, AA3 = Ala O Oarrow_forwardProline and glycine are two prevalent amino acids in the triple helix structure of collagen. Which of the following statements forms a basis for why proline and glycine are NOT as appropriate in alpha-helix structures? Alpha-helix structures are essential in fusion proteins. Gelatin, not glycine, is a prevalent amino acid in collagen. 3 of these 4 responses are correct. Proline is smaller in size, while glycine is larger in size, than a typical amino acid. Proline is larger in size, while glycine is smaller in size, than a typical amino acid.arrow_forwardFor the three peptides below, label whether they would form an amphiphilic beta-strand, amphiphilic helix, or nothing. Explain why. Part a) S-V-K-I-Q-M-R-A-D-L Part b) A-L-E-H-M-F-R-Y-L-A-K Part c) A-L-A-I-W-F-P-D-R-K-Earrow_forward
- Which of the following statements are true? The local folding of the polypeptide in some regions gives rise to the secondary structure of the protein. The most common secondary structures are the α-helix and β-pleated sheet structures. Certain amino acids have a propensity to form an α-helix, while others have a propensity to form a β-pleated sheet. Select the correct answer below: 1 and 2 1 and 3 2 and 3 all of the abovearrow_forwardWhat is the driving force that promotes secondary structure formation of alpha helices and beta sheets? How is this force arranged to make an alpha helix or beta sheet? What promotes turns or kinks in these structures? You can describe and/or draw it but please show what are the interactions facilitating this effect.arrow_forwardFluorescent proteins like the green fluorescent protein (GFP) found in jellyfish are a class of colorful proteins that shine a particular color when exposed to ultraviolet light. These proteins, despite exhibiting a wide range of diverse colors, have nearly identical secondary structure across organisms and phenotypes. Each GFP-like protein has a few alpha-helices as well as a characteristic beta-barre composed of 11 beta-sheets that shields the inside of the protein from solvent (i.e., water). The GFP like protein shown below is a green fluorescent protein from the great star coral Montastraea cavernosa and contains two alpha-helices in its structure (labeled A and B and colored cyan). A 1. Helix A contains 6 amino acids, including a phenylalanine and an aspartic acid. Which position (1 or 2, colored in red) would you more likely expect aspartic acid to be located? [ Select ] 2. If you were to compare helix A to helix B, would you expect the ratio of polar:non-polar residues to be…arrow_forward
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