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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Chapter 5, Problem 8IQ
Now that you have gained experience with concept maps, create your own map to review what you have learned about proteins. Try to include the concepts of structure and function and look for cross-links on your map. Because proteins are complex, you may want to make several smaller maps to organize your knowledge. One version of a large protein concept map is included in the answer section, but remember that the real value is in the thinking process you must go through to create your own.
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There are four levels of protein structures. Name those four levels and briefly describe them
In 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? ____________________
In your own words 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.
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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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- Give at least 10 functions of protein and describe each function. Cite an example for each function if there are any.arrow_forwardRefer to the figure below, what are the following forces of attraction is involved in the protein folding for each number. 1. 2. CH₂ C-OH CH₂ 3. 4. CH H₂C CHS H₂C CH3 CH CH₂-S S-CH₂ 3 –CH,CH,CH, CH, NHarrow_forwardDetermine the number of proteins composed of 100 Amino acid... The solution read: total proteins composed of 100 nucleotides is equal to 20100 The solution should read total proteins composed of 100 Amino acids is equal to 20100 I did have someone answer me earlier about how to obtain the solution, however, I just believe there is a typo is the solution text. We are not looking for nucleotides, we are looking for Amino acids. So it should read total proteins composed of 100 amino acids is equal to 20100. If we were looking for nucleotides it would read 4100arrow_forward
- Physical methods are often used to determine protein conformation. Describe how x-ray crystallography, cryo electron microscopy, and NMR spectroscopy can be used to determine the shapes of proteins. What are the advantages and disadvantages of each method? Which is better for small proteins? Large proteins? Huge macromolecular assemblies?arrow_forwardExplain what the protein folding problem is and why it is so difficult to predict protein structures from just their primary sequence. Highlight some of the specific challenges with your knowledge of protein secondary and tertiary structures. How would artificial intelligence or machine learning help with the de novo prediction of protein structures in the near future?arrow_forwardSelect the true statements about protein secondary structure. In an a-helix, the side chains are located on the outside of the helix. The secondary level of protein structure refers to the spatial arrangements of short segments of the protein. In a B-pleated sheet, the side chains are located between adjacent segments. Peptide bonds stabilize secondary structure. The x-helix is held together by hydrogen bonds between the amide N-H and C=O groups. Incorrectarrow_forward
- What is the FIBROUS PROTEIN as the classification of proteins based on shape or conformation? Please do not plagiarize from the internet and provide your references.arrow_forwardWhich 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 interactionsarrow_forwardDiscuss 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_forward
- Describe how a polypeptide can fold to become a functioning protein. Be sure to address the four levels of protein (folding or organization known as hierarchy of structure). In addition, describe three different jobs proteins can perform if the protein has the correct shape.arrow_forwardA protein in its native three dimensional conformation is cleaved with trypsin. According to the amino acid sequence, there are 9 residues where trypsin could cleave, yet only 3 fragments were produced from the digest. What conclusion can be made about protein structure that would lead to this result? The protein has multiple domains b. The protein is highly compacted, minimally accessible by solvent molecules c. The protein has quaternary structure d. The protein has a dynamic structure, highly accessible by solvent molecules e. The protein is compromised only of alpha helicesarrow_forwardIn order to study protein structures and functions, many protein techniques have been developed for specific applications. Which of the following pair of technique: application is INCORRECT? O a. O b. O C. O d. ELISA: protein molecular weight SDS-PAGE: protein molecular weight NMR: protein structure Peptide mass fingerprinting: protein presence and identification e. X-ray crystallography: protein structurearrow_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