Campbell Essential Biology with Physiology (5th Edition)
5th Edition
ISBN: 9780321967671
Author: Eric J. Simon, Jean L. Dickey, Jane B. Reece, Kelly A. Hogan
Publisher: PEARSON
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Textbook Question
Chapter 3, Problem 10SQ
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?
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Check out a sample textbook solutionStudents have asked these similar questions
Figure 7 shows one additional type of bond that can stabilize the tertiary structure of a
protein. This bond is called a disulfide bond (or disulfide bridge), and it involves the
sulfhydryl (-SH) R groups from one particular type of amino acid. A disulfide bond can
form only under certain conditions (oxidative conditions). We'll talk about oxidation and
reduction next week. For now, just note that this type of bond does exist in some
proteins.
Answer the below questions on tertiary structure in your own document.
8. Figure 6 shows examples of bonds that might stabilize the tertiary structure of a
protein (labeled A, B, and C). Do these interactions involve only the amino acid R
groups, only the polypeptide backbone atoms, or both?
9. In the table below, indicate what type of bond/ interaction is represented in
the examples shown in Figure 6, panels A, B, and C and whether each
interaction involves group or backbone atoms.
Example
Type of Bonding Interaction
R group or backbone?
A
В
10.…
What exactly are proteins?What is a protein's building block? What are its chemical properties?How do proteins get denatured structurally? Explain it.What does it mean to have an isoelectric point? What is the significance of it?
strictly no plagiarism.
Hair is made of protein. The protein is a structural protein called α-keratin, which contains many disulfide (S-S) bridges formed from sulfhydryl functional groups found amongst amino acids radical groups. Based on how the protein folds, the radical groups have opportunities to generate multiple disulfide bridges. The greater the number of disulfide bridges, the more tightly the hair is coiled.
Using your knowledge of proteins, write a brief paragraph theocratizing how sodium hydroxide is used in hair products to straighten hair
Chapter 3 Solutions
Campbell Essential Biology with Physiology (5th Edition)
Ch. 3 - Prob. 1SQCh. 3 - Monomers are joined together to form larger...Ch. 3 - Prob. 3SQCh. 3 - Prob. 4SQCh. 3 - When two molecules of glucose (C6H12O6) are joined...Ch. 3 - One molecule of dietary fat is made by joining...Ch. 3 - Prob. 7SQCh. 3 - Prob. 8SQCh. 3 - Prob. 9SQCh. 3 - Most proteins can easily dissolve in water....
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- The 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_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_forwardDraw the protein folding pattern when the polypeptide is immersed in water and in oil. Justify your answers by using chemical explanations. In the structure, point all possible types of intramolecular forces of attraction possible for this polypeptide in the indicated solvent system and discuss each. Discuss your answer H3N*-ala-ile-trp-arg-gly-ala-his-tyr-trp-gly-gly-tyr-arg-ile-val-thr-ile-trp-cys- met-gly-ile-asp-cys-thr-glu-cys-trp-gly-cys-phe-arg-his-pro-val-phe-CO-arrow_forward
- Hydrogen bonding is important at what level of protein structure (primary, secondary, tertiary, or quarternary)? Consider what would happen if there was no hydrogen bonding and just van der Waals in this protein structure. What would you anticipate to happen to its properties? Briefly explain with examples.arrow_forwardGlycine provides structural flexibility in proteins. What is the consequence of this on protein structure?arrow_forward(a) Are all proteins polymers? What is the basie unit of protein? Explain the formation of Zwitterion in a-amino acid. (b) Count the number of peptide bonds in the below structure. -R-N-C-R-N-C-R-N-C-R-N-C- wwww H H H Harrow_forward
- 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)?arrow_forwardTogether, these monomers make up what type of polymer (macromolecule)? List at least three (broad) functions that these macromolecules can perform. What is an example protein that we’ve discussed that uses of these functions? Using R as the side chain, draw the basic structure of an amino acid.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
- All proteins have primary (1°), secondary (2°) and tertiary (3°) structure. In addition, some (but not all) proteins exhibit quaternary (4°) structure. Explain quaternary structure and why only some proteins exhibit that level of structure.arrow_forwardPart B Assume a protein is composed of 120 amino acid residues and that each amino acid can have three possible orientations. How many total possible orientations are there for the protein? Express the number of possible orientations to three significant figures. —| ΑΣΦ 1.797 • 1057 Each possible orientation of an amino acid is due to rotation about a bond. Since there are two terminal amino acids, there will be one fewer peptide bond compared to the number of amino acids. No credit lost. Try again. Submit ? Previous Answers Request Answer orientationsarrow_forwardWhy 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_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