CAMPBEL BIOLOGY:CONCEPTS & CONNECTIONS
10th Edition
ISBN: 9780136538820
Author: Taylor
Publisher: INTER PEAR
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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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Students have asked these similar questions
Most proteins can easily dissolve in water. Knowing that, where within the overall three-dimensional shape of a protein would you most likely find hydrophobic amino acids?
How 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.
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.
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Chapter 3 Solutions
CAMPBEL BIOLOGY:CONCEPTS & CONNECTIONS
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- 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.arrow_forwardOne 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.arrow_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_forward
- Many transmembrane proteins have a large series of hydrophobic amino acids such as those in the middle of the protein (around b). Why would this make sense, and where would you expect these to be located in the final protein structure?arrow_forwardWhy is the ionic bond between, say, the side chain of lysine and the side chain of glutamic acid stronger in the hydrophobic interior of a protein than in aqueous solvent (water)?arrow_forwardA protein with a quaternary structure is a multidomain protein. Is this always correct? Explain.arrow_forward
- The addition of ethanol, CH3CHOH, t an aqueous solution lowers the surface tension of the solution. Predict whether adding ethanol to an aqueous protein solution will tend to stabilize or unfold the protein. Briefly explain.arrow_forwardProtein Structure Describe the four levels of protein structure: Primary, secondary, tertiary, and quarternary.arrow_forwardIn general, proteins can be classified into 3 different groups. Name and give a short description of each type and how they are distinct from one another. Provide an example of macromolecule or other complex structure representing each of the three types.arrow_forward
- Consider 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_forwardIn 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_forwardWhy should the BRCA1 protein be considered one of the best macromolecules within proteins? Is BRCA1 the best functionally, structurally, or based on other properties? Please explain in detail. You can give examples with scientific articles related to protein.arrow_forward
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