Essentials of Genetics (9th Edition) - Standalone book
9th Edition
ISBN: 9780134047799
Author: William S. Klug, Michael R. Cummings, Charlotte A. Spencer, Michael A. Palladino
Publisher: PEARSON
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Chapter 13, Problem 10PDQ
Summary Introduction
To review:
The level of protein organization of hemoglobin protein if it is a tetramer of two alpha and two beta-chains.
Introduction:
Protein molecules are made up of amino acid as the monomer units. The kind of amino acids that form a polypeptide chain determine the charge of the protein thus formed and also its shape. This is because amino acid residues help in protein folding by the formation of bonds such hydrogen bonds and disulfide bridges. Protein folding is important for the protein to carry out its function. A misfolded protein is rendered useless. Hemoglobin is a protein of the red blood cells that carries oxygen to different tissues of the body.
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Hemoglobin is a tetramer consisting of two α and two β chains.What level of protein structure is described in this statement?
Identify the following statements as descriptive of the secondary, tertiary, or quaternary structure of a protein. What types of interactions stabilize each type of structure?(a) The polypeptide chain has a number of bends and twists, resulting in a compact structure.(b) The polypeptide backbone forms a right-handed coil.(c) The four polypeptide chains are arranged in a spherical shape.
A protein with a quaternary structure is a multidomain protein. Is this always correct? Explain.
Chapter 13 Solutions
Essentials of Genetics (9th Edition) - Standalone book
Ch. 13 - CASE STUDY | Crippled ribosomes Diamond Blackfan...Ch. 13 - CASE STUDY | Crippled ribosomes Diamond Blackfan...Ch. 13 - Prob. 3CSCh. 13 -
HOW DO WE KNOW?
1. In this chapter, we focused on...Ch. 13 - Review the Chapter Concepts list on p. 238. These...Ch. 13 - List and describe the role of all molecular...Ch. 13 - Contrast the roles of tRNA and mRNA during...Ch. 13 - Francis Crick proposed the adaptor hypothesis for...Ch. 13 -
6. During translation, what molecule bears the...Ch. 13 - Summarize the steps involved in charging tRNAs...
Ch. 13 - Each transfer RNA requires at least four specific...Ch. 13 -
9. Explain why the one-gene:one-enzyme hypothesis...Ch. 13 - Prob. 10PDQCh. 13 - Prob. 11PDQCh. 13 - Prob. 12PDQCh. 13 - Assuming that each nucleotide is 0.34 nm long in...Ch. 13 - Review the concept of colinearity in Section 12.5...Ch. 13 -
15. In your opinion, which of the four levels of...Ch. 13 -
16. List and describe the function of as many...Ch. 13 - How does an enzyme function? Why are enzymes...Ch. 13 -
18. Shown in the following table are several...Ch. 13 -
19. Three independently assorting genes are known...Ch. 13 -
20. How would the results in cross (a) of Problem...Ch. 13 - A series of mutations in the bacterium Salmonella...Ch. 13 -
22. The emergence of antibiotic-resistant strains...
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- Proteins are composed of both polar (hydrophilic) and nonpolar (hydrophobic) amino acids. Assume you are starting with fresh homogenized/pasteurized cow's milk. A major protein in the milk is a whey protein known as alpha-lactalbumin (in a tertiary structure). If this protein is denatured (for example by the introduction of heat, acid, or other means), discuss how and why scientifically it could end up becoming an effective emulsifier in a product containing olive oil and red wine vinegar.arrow_forwardhow does the protein environment surrounding an amino acid chain affect its chemical properties?Consider the carboxyl group on an asparate side chain in the following environments in a protein. Rank in order these environments from the highest to the lowest proportion of carboxyl groups in the -COO- form.that is in terms of pKas. 1. an aspartate side chain on the surface of protein with no other ionizable groups nearby. 2. an aspartate side chain buried in a hydrophobic pocket on the surface of a protein 3. an asparate chain in a hydrophobic pocket adjacent to a glutamte side chain 4. an asparate side chain in a hydrophobic porket adjacent to a lysine side chain.arrow_forwardGive an example of a protein containing primarily betapleated sheets. Is this a fibrous or globular protein?arrow_forward
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- Fibrous proteins, globular proteins, and conjugated proteins are the three (3) primary kinds of proteins. Give a brief description of each kind and an example of each.arrow_forwardDraw the chemical structure of an alanine pentapeptide. Indicate the location of each peptide bond. Label the phi () and psi () dihedral angles. Name and briefly define the four levels of protein structure.arrow_forwardFor the protein given in the attached picture: Write the name of these 5 amino acids corresponding to their abbreviation of 3 letters. Describe precisely how the functional groups in the amino acids are involved in bonding between two successive amino acids in the protein.arrow_forward
- A) List each of the five major functional classes of proteins. B) Discuss the function for each class, give an example of a protein for each class and mention how the function of the protein example fits the function of the class (40 words or less for each class with its examplearrow_forwardProtein folding is critical for function because the properties of a protein arise from its overall shape and the distribution within that shape of the various amino acid side-chains. Which of the following statements about protein three-dimensional structure are correct? 1) the folding pattern of a protein is ultimately determined by its amino acid sequence. 2) proteins tend to fold in such a way that the hydrophobic amino acids are buried in the interior, while hydrophilic amino acids are exposed at the surface. 3) the chemical interactions within a protein molecule that support its overall folded structure are mostly covalent C-C (carbon to carbon) bonds between amino acid side-chains. 4) the overall folding pattern/shape of a protein molecule is termed its primary structure. 5) during evolution, the three-dimensional structure of a protein is often more strongly conserved than its amino acid sequence. More than one answer might be rightarrow_forwardTripeptides are composed of three amino acids linked by peptide bonds. Given a set of amino acids, you can make several different tripeptides.(a) Use the three-letter shorthand notations to name all the tripeptides that can be made from serine, tyrosine, and glycine. Each amino acid will be used once in each tripeptide.(b) Draw the complete structure of the tripeptides that have glycine as the N-terminal amino acid.arrow_forward
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