What do you think holds together the various secondary structural elements in a particular three-dimensional pattern? (Hint: Look back at Figure 4 - what is

Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
icon
Related questions
Question
**Question 7:** What do you think holds together the various secondary structural elements in a particular three-dimensional pattern? (Hint: Look back at Figure 4 - what is sticking out from the sides of the α-helices and β-strands?)

---

**Figure 6 Explanation:**

The diagram illustrates three examples of bonding interactions that stabilize the tertiary structures of proteins, marked by arrows A, B, and C.

- **Arrow A (Glutamic Acid & Lysine Interaction):** This image shows a hydrogen bonding or ionic interaction between the side chains of glutamic acid and lysine. These interactions are essential for stabilizing protein structure.
  
- **Arrow B (Valine & Alanine Interaction):** This part of the figure displays a hydrophobic interaction between nonpolar side chains such as valine and alanine. These interactions help proteins fold into their native structures by minimizing exposure to aqueous environments.
  
- **Arrow C:** This section probably highlights another type of intramolecular bond, such as a hydrogen bond within the protein backbone, emphasized by “R” groups protruding to the side.

**Figure 7 Explanation:**

The figure describes the formation and breaking of disulfide bonds within proteins, which are covalent bonds formed between sulfur atoms (S-S) in cysteine residues, contributing to protein stability.

- **Oxidative Environment:** Promotes the formation of disulfide bonds, as shown by the left-pointing arrow.
  
- **Reducing Environment:** Leads to the breaking of disulfide bonds, indicated by the right-pointing arrow.

**Source Details:**

- Figure 6 and 7 are sourced from the 4th Edition of *Essential Cell Biology* by Alberts et al. (2013), reproduced with permission from Garland Science/Taylor & Francis LLC.
Transcribed Image Text:**Question 7:** What do you think holds together the various secondary structural elements in a particular three-dimensional pattern? (Hint: Look back at Figure 4 - what is sticking out from the sides of the α-helices and β-strands?) --- **Figure 6 Explanation:** The diagram illustrates three examples of bonding interactions that stabilize the tertiary structures of proteins, marked by arrows A, B, and C. - **Arrow A (Glutamic Acid & Lysine Interaction):** This image shows a hydrogen bonding or ionic interaction between the side chains of glutamic acid and lysine. These interactions are essential for stabilizing protein structure. - **Arrow B (Valine & Alanine Interaction):** This part of the figure displays a hydrophobic interaction between nonpolar side chains such as valine and alanine. These interactions help proteins fold into their native structures by minimizing exposure to aqueous environments. - **Arrow C:** This section probably highlights another type of intramolecular bond, such as a hydrogen bond within the protein backbone, emphasized by “R” groups protruding to the side. **Figure 7 Explanation:** The figure describes the formation and breaking of disulfide bonds within proteins, which are covalent bonds formed between sulfur atoms (S-S) in cysteine residues, contributing to protein stability. - **Oxidative Environment:** Promotes the formation of disulfide bonds, as shown by the left-pointing arrow. - **Reducing Environment:** Leads to the breaking of disulfide bonds, indicated by the right-pointing arrow. **Source Details:** - Figure 6 and 7 are sourced from the 4th Edition of *Essential Cell Biology* by Alberts et al. (2013), reproduced with permission from Garland Science/Taylor & Francis LLC.
**Transcription for Educational Website:**

---

4. Do the “Bond X” bonds in Figure 4 involve atoms in the amino acid R groups or in the polypeptide “backbone”/“main chain” atoms?

5. Given Your Answer To “b,” are each of the following statements True or False? Be able to explain your reasoning.

   - Only very specific primary sequences can form α-helices and β-sheets.
   
   - Many different primary sequences can form α-helices and β-sheets.

Each arrow depicted in Figure 4D represents consecutive amino acids in the primary sequence of the polypeptide, while the different arrows may be formed from amino acids that are removed from each other in the primary sequence. Each arrow is referred to as a β-strand, and the structure formed through interaction of the β-strands is the β-sheet. In a complete protein, other segments of the protein would connect the different β-strands.

6. Do the “Bond X” bonds in the β-sheet connect atoms from the same β-strand or neighboring strands?

**TERTIARY STRUCTURE**

**Figure 5.** Examples of the arrangement of α-helices and β-sheets in folded protein domains. Copyright 2013 from *Essential Cell Biology*, 4th Edition by Alberts et al. Reproduced by permission of Garland Science/Taylor & Francis LLC.

Figure 5 shows three examples of how secondary structure elements can be arranged in relation to one another in the functional, folded form of a complete protein or one compact portion of a protein. The overall three-dimensional shape (or conformation) of a protein is its *tertiary structure*.

**Graphs and Diagrams Explanation:**

- **Figure 5 Diagram (A):** Displays a structure composed predominantly of α-helices depicted as spirals or cylinders.
  
- **Figure 5 Diagram (B) and (C):** Illustrate structures comprising both α-helices (green) and β-sheets (red). The β-sheets are represented by the red arrows, which show the directionality of the polypeptide strands in the sheet formation.

These figures demonstrate different ways in which protein segments can fold to form stable tertiary structures that are essential for protein function.
Transcribed Image Text:**Transcription for Educational Website:** --- 4. Do the “Bond X” bonds in Figure 4 involve atoms in the amino acid R groups or in the polypeptide “backbone”/“main chain” atoms? 5. Given Your Answer To “b,” are each of the following statements True or False? Be able to explain your reasoning. - Only very specific primary sequences can form α-helices and β-sheets. - Many different primary sequences can form α-helices and β-sheets. Each arrow depicted in Figure 4D represents consecutive amino acids in the primary sequence of the polypeptide, while the different arrows may be formed from amino acids that are removed from each other in the primary sequence. Each arrow is referred to as a β-strand, and the structure formed through interaction of the β-strands is the β-sheet. In a complete protein, other segments of the protein would connect the different β-strands. 6. Do the “Bond X” bonds in the β-sheet connect atoms from the same β-strand or neighboring strands? **TERTIARY STRUCTURE** **Figure 5.** Examples of the arrangement of α-helices and β-sheets in folded protein domains. Copyright 2013 from *Essential Cell Biology*, 4th Edition by Alberts et al. Reproduced by permission of Garland Science/Taylor & Francis LLC. Figure 5 shows three examples of how secondary structure elements can be arranged in relation to one another in the functional, folded form of a complete protein or one compact portion of a protein. The overall three-dimensional shape (or conformation) of a protein is its *tertiary structure*. **Graphs and Diagrams Explanation:** - **Figure 5 Diagram (A):** Displays a structure composed predominantly of α-helices depicted as spirals or cylinders. - **Figure 5 Diagram (B) and (C):** Illustrate structures comprising both α-helices (green) and β-sheets (red). The β-sheets are represented by the red arrows, which show the directionality of the polypeptide strands in the sheet formation. These figures demonstrate different ways in which protein segments can fold to form stable tertiary structures that are essential for protein function.
Expert Solution
trending now

Trending now

This is a popular solution!

steps

Step by step

Solved in 2 steps

Blurred answer
Similar questions
Recommended textbooks for you
Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
Biology
ISBN:
9780134580999
Author:
Elaine N. Marieb, Katja N. Hoehn
Publisher:
PEARSON
Biology 2e
Biology 2e
Biology
ISBN:
9781947172517
Author:
Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher:
OpenStax
Anatomy & Physiology
Anatomy & Physiology
Biology
ISBN:
9781259398629
Author:
McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa Stouter
Publisher:
Mcgraw Hill Education,
Molecular Biology of the Cell (Sixth Edition)
Molecular Biology of the Cell (Sixth Edition)
Biology
ISBN:
9780815344322
Author:
Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter Walter
Publisher:
W. W. Norton & Company
Laboratory Manual For Human Anatomy & Physiology
Laboratory Manual For Human Anatomy & Physiology
Biology
ISBN:
9781260159363
Author:
Martin, Terry R., Prentice-craver, Cynthia
Publisher:
McGraw-Hill Publishing Co.
Inquiry Into Life (16th Edition)
Inquiry Into Life (16th Edition)
Biology
ISBN:
9781260231700
Author:
Sylvia S. Mader, Michael Windelspecht
Publisher:
McGraw Hill Education