Study Guide for Campbell Biology
11th Edition
ISBN: 9780134443775
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Jane B. Reece, Martha R. Taylor, Michael A. Pollock
Publisher: PEARSON
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Textbook Question
Chapter 5, Problem 7IQ
In the following diagram of a portion of a protein, label the types of interactions that are shown. What level of structure are these interactions producing?
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Consider protein folding that results when the following components interact:
Where the solution is at a pH of 7, green (thick-dotted line) represents aspartic acid (R group contains a carboxylic acid with pKa = 4), orange (thick-solid line) represents lysine (R group contains an amine with pKa = 10), and blue (thin-solid line) represents hydrophilic groups.
Rank the three complexes in order from lowest to highest dissociation constants Kd (low Kd values correspond to good binding constants and low energy, while high Kd values correspond to low binding constants and high energy) as determined by intermolecular charge-charge interactions. For those complexes with charge-charge interactions being equal, look at the possibility for the formation of hydrogen bonds via carboxylic acid dimers (only possible when the carboxylic acid is protonated) which are low energy structures.
Why is the 3-Dimensional structure important for protein function?
What factors or agents can denature protein structure? Give examples (more than one factor)
Why denaturation affect the function of proteins? Explain the structure - function relationship.
One technique that is used when attempting to solve the crystal structure of a large protein is not to solve the structure of the whole protein itself. Instead, the protein is
broken down into smaller components and the structure of the smaller components is what is solved. Of course, when performing this technique, it must be ensured that
the process of breaking down the protein into smaller components does not drastically change the structure of the smaller components. With this in mind, where would be
the best locations to cut a protein?
At the beginning and end of secondary structures.
At beginning and end of protein domains.
O At the beginning and end of motifs.
At the beginning and end of protein subunits.
Chapter 5 Solutions
Study Guide for Campbell Biology
Ch. 5 - Monomers are linked into polymers by ________...Ch. 5 - You can recognize a monosaccharide by its multiple...Ch. 5 - Number the carbons in the following glucose and...Ch. 5 - Prob. 4IQCh. 5 - Fill in this concept map to help you organize your...Ch. 5 - a. Draw the amino acids alanine (R group: CH3) and...Ch. 5 - In the following diagram of a portion of a...Ch. 5 - Now that you have gained experience with concept...Ch. 5 - a. Label the three parts of this nucleotide....Ch. 5 - Take the time to create a concept map that...
Ch. 5 - Prob. 1SYKCh. 5 - Prob. 2SYKCh. 5 - glycogen A. carbohydrate B. lipid C. protein D....Ch. 5 - cholesterol A. carbohydrate B. lipid C. protein D....Ch. 5 - RNA A. carbohydrate B. lipid C. protein D. nucleic...Ch. 5 - collagen A. carbohydrate B. lipid C. protein D....Ch. 5 - hemoglobin A. carbohydrate B. lipid C. protein D....Ch. 5 - A. carbohydrate B. lipid C. protein D. nucleic...Ch. 5 - Prob. 7TYKMCh. 5 - enzyme A. carbohydrate B. lipid C. protein D....Ch. 5 - cellulose A. carbohydrate B. lipid C. protein D....Ch. 5 - Chitin A. carbohydrate B. lipid C. protein D....Ch. 5 - Polymerization (the formation of polymers) is a...Ch. 5 - Which of the following statements is not true of a...Ch. 5 - Prob. 3TYKCh. 5 - Prob. 4TYKCh. 5 - Prob. 5TYKCh. 5 - Prob. 6TYKCh. 5 - A fatty acid that has the formula C16H32O2 is a....Ch. 5 - Prob. 8TYKCh. 5 - Prob. 9TYKCh. 5 - Prob. 10TYKCh. 5 - Which of the following molecules provides the most...Ch. 5 - Prob. 12TYKCh. 5 - What happens when a protein denatures? a. Its...Ch. 5 - The helix of proteins is a. part of a proteins...Ch. 5 - What is the best description of the following...Ch. 5 - Prob. 16TYKCh. 5 - Prob. 17TYKCh. 5 - Which of the following is true of the subunits of...Ch. 5 - Prob. 19TYKCh. 5 - If the nucleotide sequence of one strand of a DNA...Ch. 5 - How are nucleotide monomers connected to form a...Ch. 5 - Prob. 22TYK
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- Describe the forces that are involved in the tertiary structure of a protein and give an example of each force listed.arrow_forwardName two(2) interactions that maintain tertiary protein structure.arrow_forwardDrag each of the following items into the corresponding boxes to indicate the protein structural level that is predominantly affected by the chemical interactions listed. Some items may be placed in more than one box. Reset Help Hydrogen bonds between polar groups in amino acid side chains Hydrophobic interactions between amino acid side chains lonic bonds between positively- charged and negatively-charged amino acid side chains Peptide bonds Hydrogen bonds between carbonyl oxygens and amino nitrogens within a polypeptide backbone Disulfide bonds Primary structure Seconday structure Tertiary structure Quaternary structurearrow_forward
- Discuss the different structures (primary, secondary, tertiary, and Quaternary structures) of protein. What are the five factors that promote protein folding and stability. (Hint: One factor is the Hydrogen bond). Extra Hint: Another factor is the Hydrophobic effect.arrow_forwardThe following figure is a diagram (cartoon or caricature) of the structure of a protein. What types of secondary structure are observed in the molecule? Is it a globular protein or a fibrous one?arrow_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_forward
- In a subunit of a protein, arginine and aspartic acid have an ionic interaction between their side chains. Part a) If arginine is changed to glutamic acid, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why. Part b) If arginine is changed to lysine, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why. Part c) If arginine is changed to isoleucine, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why.arrow_forwardProtein 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_forwardIf a quaternary (4°) protein structure has six N-terminus. How many total subunits does it have?arrow_forward
- Draw 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_forwardConsider the protein below: HO HỘ NH CH-OH CH Identify/Name the noncovalent interaction between groups in the following locations: Σarrow_forwardOftentimes, the major challenge in the determination of protein structure via X-ray crystallography is the production of good crystals. One common approach is to crystallize fragments of the whole protein instead of crystallizing the whole protein. If you were to cleave a protein into fragments that will still retain the folding of that fragment in the whole protein, where is the best location to perform the cleavage? O At the ends of each alpha helix. O At the ends of a protein motif. O At the points connecting protein domains. O At the ends of beta strands.arrow_forward
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Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY