Modified Mastering Biology with Pearson eText -- Standalone Access Card -- for Campbell Biology: Concepts & Connections (9th Edition)
9th Edition
ISBN: 9780134641683
Author: Martha R. Taylor, Eric J. Simon, Jean L. Dickey, Kelly A. Hogan, Jane B. Reece
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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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?
Why 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)?
Amino acids are ionic compounds, very soluble in water. Proteins, however, which are made up of amino acids are much less soluble, and must be folded up very precisely to maximize their solubility. Why are proteins so much less soluble than the amino acids of which they are made?
Chapter 3 Solutions
Modified Mastering Biology with Pearson eText -- Standalone Access Card -- for Campbell Biology: Concepts & Connections (9th Edition)
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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_forwardBelow is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the N-terminus and C-terminus. Draw a box around the peptide bonds.arrow_forwardA protein with a quaternary structure is a multidomain protein. Is this always correct? Explain.arrow_forward
- Why do small proteins have more difficulty folding and holding shape than larger proteins? If you were designing a small protein, what elements of structure might you include to increase protein stability?arrow_forwardProtein structure is determined solely by a protein’s amino acid sequence. Should a genetically engineered protein in which the original order of all amino acids is reversed have the same structure as the original protein?arrow_forwardGlobular proteins are typically constructed from several layers of secondary structure, with a hydrophobic core and a hydrophilic surface. Is this true for a fibrous protein such as keratin?arrow_forward
- 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? ____________________arrow_forwardProteins are polymers of amino acids that fold in which three dimensions?arrow_forwardMany 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_forward
- 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_forwardAt what level of protein structure (primary, secondary, tertiary or quarternary) does Hydrogen bonding is relevant ? Consider if there is no Hydrogen bonding that exists, and only van der Waals exists in this protein structure, what do you expect to happen in its property? Explain with examples.arrow_forwardProtein Structure Describe the four levels of protein structure: Primary, secondary, tertiary, and quarternary.arrow_forward
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