Biology: Life on Earth
10th Edition
ISBN: 9780321729712
Author: Gerald Audesirk, Teresa Audesirk, Bruce E. Byers
Publisher: Benjamin Cummings
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Chapter 3, Problem 3FTB
Fill-in-the-Blank
Proteins are synthesized by a reaction called_________ synthesis, which releases_________. Subunits of proteins are called__________. The sequence of protein subunits is called the_______ structure of the protein. Two regular configurations of secondary protein structure are________ and_________. Which of these secondary structures is characteristic of infectious prion proteins?________ When a protein's secondary or higher-order structure is destroyed, the protein is said to be________. LO5 LO6
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Proteins are synthesized by a reaction called__________synthesis, which releases______________ . Subunits of proteins are called________ . The sequence of protein subunits is called the_________ structure of the protein. Two regular configurations of secondary protein structure are__________ and________ . When a protein’s secondary or higher-order structure is destroyed, the protein is said to be__________ .
In protein synthesis, adenine pairs with ________________________, and guanine pairs with ________________________.
Multiple Choice
uracil; cytosine
adenine; guanine
None of the answer choices are correct.
thymine; cytosine
thymine; uracil
Which statement about quaternary structure is TRUE?
Quaternary structure is unaffected by acids or heat.
Quaternary structure is determined by the same interaction that holds an α-helix together.
Quaternary structure is how prosthetic groups are held in a protein.
Quaternary structure is the position of subunits in the overall structure of a protein.
All proteins have quaternary structure
Chapter 3 Solutions
Biology: Life on Earth
Ch. 3 - Fill-in-the-Blank In organic molecules made of...Ch. 3 - 5. Fill in the following with the appropriate type...Ch. 3 - Fill-in-the-Blank Proteins are synthesized by a...Ch. 3 - Fill-in-the-Blank Till in the following with the...Ch. 3 - Fill-in-the-Blank A nucleotide consists of three...Ch. 3 - Prob. 1RQCh. 3 - List the four principal classes of biological...Ch. 3 - What roles do nucleotides play in living...Ch. 3 - Prob. 4RQCh. 3 - Prob. 5RQ
Ch. 3 - Prob. 6RQCh. 3 - Describe the synthesis of a protein from amino...Ch. 3 - Where in nature do we find cellulose? Where do we...Ch. 3 - Which kinds of bonds between keratin molecules are...Ch. 3 - In this chapter, you read that a phospholipid has...Ch. 3 - Prob. 2ACCh. 3 - Some people think that consuming fat and sugar...Ch. 3 - Saliva from infected deer can transmit chronic...Ch. 3 - In an alternate universe where people could digest...
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- Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternaryarrow_forwardWhich of the following statements is not true about protein folding ? * Protein folding is a process by which a polypeptide chain form a stable 3D structure. Protein folding leads to loss of function and causes a wide range of diseases When protein is defolded, peptide bonds are not affected. Protein folding is essential for proper function of proteins.arrow_forwardGive at least 10 functions of protein and describe each function. Cite an example for each function if there are any.arrow_forward
- List and describe four levels of protein structure and give examplesarrow_forwardIn the following diagram of a portion of a protein, label the types of interactions that are shown. What level of protein structure are these interactions producing? ____________________arrow_forwardAt what level of protein structure (primary, secondary, tertiary, or quaternary) will protein structure be initially altered? Heating a protein (due to fever), causing hydrogen bonds to break. Drastic changes in pH (like the above patients), causing some polar amino acids to turn into non-polar amino acidsarrow_forward
- draw a model of a protein Include a brief description of your protein - what protein is it? what details can you share about this protein (for example, a description of it's shape, how big it is (either in kilodaltons or number of amino acids), what is its function)arrow_forwardDuring the folding of a protein in a buffered aqueous solution, what happens to the entropy of the protein and the entropy of the water? The entropy of the protein decreases while the entropy of the water increases. Both the entropy of the protein and the entropy of the water increase. Both the entropy of the protein and the entropy of the water decrease. The entropy of the protein decreases while the entropy of the water remains constant.arrow_forwardList the four levels of protein structure and briefly explain the factors that contribute to each level.arrow_forward
- Protein structures have several different levels of organization. In the space below indicate the type of molecular bonds that can contribute to each level of organization: primary- secondary- tertiary- quarternary-arrow_forwardThere is a "primary driving force" behind protein folding (to form tertiary structure). This driving force can be used to explain below phenomenon except: water has a high density and a high boiling temperature non-polar amino acids go inside a protein long chain fatty acids form micelles oil spills go to the surface of water phospholipids form lipid bilayerarrow_forwardWhich of the following statements about protein folding is incorrect? Select all. GroEL/GroES allow unfolded proteins the chance to fold within an isolated cavity. Heat shock proteins bind to regions of unfolded polypeptides that are rich in hydrophobic residues, preventing inappropriate aggregation. Many molecular chaperones require ATP for proper function. Molecular chaperones are required for the folding of all cellular proteins.arrow_forward
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