. Vwhat do you think holds together the various secondary structural elements in a Stickular three-dimensional pattern? (Hint: Look back at Figure 4 - what is Sticking out from the sides of the a-helices and B-strands?) glutamic acid H N-C-C -C-Cーや CH2 C. CH2 H C=0 CH CH C-C-H valine CHI CH H-N CH H
. Vwhat do you think holds together the various secondary structural elements in a Stickular three-dimensional pattern? (Hint: Look back at Figure 4 - what is Sticking out from the sides of the a-helices and B-strands?) glutamic acid H N-C-C -C-Cーや CH2 C. CH2 H C=0 CH CH C-C-H valine CHI CH H-N CH H
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,...
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
Transcribed Image Text:**Transcription of Educational Content on Protein Structures and Bonding**
**Text Description:**
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?*)
**Diagrams and Explanations:**
**Figure 4-4:** Illustrates three examples of bonding interactions that stabilize the tertiary structures of proteins, indicated by arrows A, B, and C. This diagram shows different side chains interacting:
- **Arrow A:** Glutamic acid interacts with lysine through ionic bonding, facilitated by the positive charge on lysine and the negative charge on glutamic acid.
- **Arrow B:** Demonstrates hydrophobic interactions between nonpolar side chains such as valine and alanine. The circled CH₃ groups indicate hydrophobic clustering.
- **Arrow C:** Indicates hydrogen bonding between peptide backbones.
**Figure 6:** Diagram shows two identical polypeptide segments with disulfide bonds. It highlights the process of disulfide bond formation through oxidation, and bond breaking through reduction.
**Figure 7:** Depicts disulfide bonds within proteins that can form (left-pointing arrow) or be broken (right-pointing arrow), depending on their chemical surroundings (oxidative or reducing).
**Copyright Information:**
Both figures are from the 2013 edition of *Essential Cell Biology*, 4th Edition by Alberts et al., reproduced by permission of Garland Science/Taylor & Francis LLC.
These illustrations provide a clear depiction of the interactions that stabilize protein structures, emphasizing the roles of ionic bonds, hydrophobic interactions, hydrogen bonds, and disulfide bonds.
![**Educational Content on Tertiary Structure of Proteins**
Figure 7 introduces an important concept in protein chemistry: the disulfide bond. This bond can stabilize the tertiary structure of a protein by forming between the sulfhydryl (-SH) groups of specific amino acids. These bonds are typically formed under oxidative conditions and are crucial for the structural integrity of certain proteins.
**Discussion and Questions**
1. **Figure 6 Overview**: It presents examples of bonds (A, B, and C) that stabilize protein tertiary structure. These examples help illustrate whether interactions involve amino acid R groups, polypeptide backbone atoms, or both.
2. **Question 8**: Analyze the bonds in Figure 6. Determine if they involve R groups, backbone atoms, or both.
3. **Table to Fill**:
- Example A: [Students to fill]
- Example B: [Students to fill]
- Example C: [Students to fill]
4. **Question 10**: Consider how pH, temperature, and salt concentration impact the interactions in Figure 6. Provide explanations for each condition.
5. **Question 11**: Identify which amino acid can form disulfide bonds, referring to amino acid charts and Figure 7 for assistance.
6. **Question 12**: Compare disulfide bonds with other bonds that stabilize tertiary structures. Assess their relative strength and properties.
7. **Question 13**: Predict types of tertiary interactions in proteins from extremophiles (e.g., hot springs) versus those from moderate environments. Provide reasoning for predictions.
This content enhances understanding of biochemical interactions and prepares students for further exploration of protein chemistry.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Face0a007-9e9c-4a6a-a4cb-4907b19d1415%2F2c563e91-54c6-48c8-946d-d7c3849f709a%2Fvfolyjq_processed.jpeg&w=3840&q=75)
Transcribed Image Text:**Educational Content on Tertiary Structure of Proteins**
Figure 7 introduces an important concept in protein chemistry: the disulfide bond. This bond can stabilize the tertiary structure of a protein by forming between the sulfhydryl (-SH) groups of specific amino acids. These bonds are typically formed under oxidative conditions and are crucial for the structural integrity of certain proteins.
**Discussion and Questions**
1. **Figure 6 Overview**: It presents examples of bonds (A, B, and C) that stabilize protein tertiary structure. These examples help illustrate whether interactions involve amino acid R groups, polypeptide backbone atoms, or both.
2. **Question 8**: Analyze the bonds in Figure 6. Determine if they involve R groups, backbone atoms, or both.
3. **Table to Fill**:
- Example A: [Students to fill]
- Example B: [Students to fill]
- Example C: [Students to fill]
4. **Question 10**: Consider how pH, temperature, and salt concentration impact the interactions in Figure 6. Provide explanations for each condition.
5. **Question 11**: Identify which amino acid can form disulfide bonds, referring to amino acid charts and Figure 7 for assistance.
6. **Question 12**: Compare disulfide bonds with other bonds that stabilize tertiary structures. Assess their relative strength and properties.
7. **Question 13**: Predict types of tertiary interactions in proteins from extremophiles (e.g., hot springs) versus those from moderate environments. Provide reasoning for predictions.
This content enhances understanding of biochemical interactions and prepares students for further exploration of protein chemistry.
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