Campbell Biology: Concepts & Connections (8th Edition)
8th Edition
ISBN: 9780321885326
Author: Jane B. Reece, Martha R. Taylor, Eric J. Simon, Jean L. Dickey, Kelly A. Hogan
Publisher: PEARSON
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Textbook Question
Chapter 3, Problem 11TYK
Most proteins are soluble in the aqueous environment of a cell. Knowing that, where in the overall three-dimensional shape of a protein would you expect to find amino acids with hydrophobic R groups?
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Protein 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 right
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 3 Solutions
Campbell Biology: Concepts & Connections (8th Edition)
Ch. 3 - Complete the following table to help you review...Ch. 3 - A glucose molecule is to starch as (Explain your...Ch. 3 - What makes a fatty acid an acid? a. It does not...Ch. 3 - Prob. 4TYKCh. 3 - Of the following functional groups, which is/are...Ch. 3 - Prob. 6TYKCh. 3 - Prob. 7TYKCh. 3 - Prob. 8TYKCh. 3 - Which structural level of a protein would be least...Ch. 3 - Circle and name the functional groups in this...
Ch. 3 - Most proteins are soluble in the aqueous...Ch. 3 - Sucrose is broken down in your intestine to the...Ch. 3 - The diversity of life is staggering. Yet the...Ch. 3 - How can a cell make many different kinds of...Ch. 3 - Given that the function of egg yolk is to nourish...Ch. 3 - Enzymes usually function best at an optimal pH and...Ch. 3 - SCIENTIFIC THINKING Another aspect of the Nurses...
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- A protein with a quaternary structure is a multidomain protein. Is this always correct? Explain.arrow_forwardBiochemists talk about protein structure at four distinct levels: primary, secondary, tertiary and quaternary structure. Below are depictions of each of these levels of protein structure. For each image, match the term and the written description of the level of protein structure that the image depicts. Drag the appropriate items to their respective bins.arrow_forwardConsider two proteins, Protein A and Protein B: A is a monomeric protein, whereas B is a subunit of a homo-tetrameric protein. Both A and B are soluble. Additionally, both A and B have similar 3D structures. What differences would you expect to see between the amino acids exposed on the surfaces of A and B? Explain the reasons for the differences observed.arrow_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_forwardHow can a protein’s potential function be determined from a protein’s primary structure? I assumed this was not possible, I thought its function was determined from its 3-dimensional structure only. Thank you for explaining this.arrow_forwardYou have a soluble protein that is highly flexible and is only 23 kDa in size. What is the most suitable technique (X-ray crystallography, NMR, cryo-EM) for structure determination of this protein? Explain your reasoning.arrow_forward
- Suppose that there is a protein consisting of two polypeptide chains with the given sequences in the picture. What will be the expected result if a biochemist does an end-group analysis to identify the N and C terminal residues of the protein? Explain why.arrow_forwardDescribe as completely as possible, the four levels of protein What type of bonds hold a protein together at the primary level? What type of bonds maintain the protein at the secondary and tertiary level? Give an example of secondary, tertiary, and quarternary level proteins. At which level is the protein functional? What happens (at a molecular level) when a protein is denatured?arrow_forwardThe tertiary structure of a protein is the 3-dimensional folding of the polypeptide chain. What types of bonds support the folding of proteins into this level of protein structure? Also, how do these bonds/interactions impact how a protein folds and its surface properties? Can the tertiary structure of a protein depend on the type of cell system used for synthesis? Explain.arrow_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_forwardConsider a small protein containing 101 amino acid residues. The proteinbackbone will have 200 bonds about which rotation can occur. Assume thatthree orientations are possible about each of these bonds.(a) Based on these assumptions, about how many random-coil conformationswill be possible for this protein?(b) The estimate obtained in (a) is surely too large. Give one reason why.arrow_forwardIf a lipid raft is typically 70 nm in diameter and each lipid molecule has a diameter of 0.5 nm, about how many lipid molecules would there be in a lipid raft com- posed entirely of lipid? At a ratio of 50 lipid molecules per protein molecule (50% protein by mass), how many proteins would be in a typical raft? (Neglect the loss of lipid from the raft that would be required to accommodate the protein.)arrow_forward
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