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Question 16.a c Proteins fold into complex three-dimensional upon the structure of the protein and its cell protein is based on the identity of the ami

Question 16.a c Proteins fold into complex three-dimensional upon the structure of the protein and its cell protein is based on the identity of the ami

Chemistry
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
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**Protein Structures and Amino Acid Properties** As proteins fold into complex three-dimensional shapes, their function is dependent upon the structure of the protein and its cellular location. The final shape of the protein is dictated by the identity of the amino acid side chains of the protein. Many globular proteins are either water-soluble or partially water-soluble. Given their solubility properties, one critical question arises: What type of amino acids would you expect to find on the surface of these proteins? 1. **A) Nonpolar** 2. **B) Polar Neutral** 3. **C) Polar Acidic** 4. **D) Polar Basic** 5. **E) Any of the polar side chains** The question highlights the importance of understanding the nature of amino acid side chains and their impact on protein structure and solubility. It is essential to note that amino acids with polar side chains, which can be neutral, acidic, or basic, are typically found on the surface of water-soluble proteins. These polar amino acids facilitate the interaction of the protein with the aqueous environment, enhancing its solubility.
Transcribed Image Text:**Protein Structures and Amino Acid Properties** As proteins fold into complex three-dimensional shapes, their function is dependent upon the structure of the protein and its cellular location. The final shape of the protein is dictated by the identity of the amino acid side chains of the protein. Many globular proteins are either water-soluble or partially water-soluble. Given their solubility properties, one critical question arises: What type of amino acids would you expect to find on the surface of these proteins? 1. **A) Nonpolar** 2. **B) Polar Neutral** 3. **C) Polar Acidic** 4. **D) Polar Basic** 5. **E) Any of the polar side chains** The question highlights the importance of understanding the nature of amino acid side chains and their impact on protein structure and solubility. It is essential to note that amino acids with polar side chains, which can be neutral, acidic, or basic, are typically found on the surface of water-soluble proteins. These polar amino acids facilitate the interaction of the protein with the aqueous environment, enhancing its solubility.
## Understanding Protein Structure and Interactions **Proteins have complex three-dimensional structures.** These polymers are held into these specific shapes with a variety of intermolecular forces, covalent bonds, and ionic bonds. **Proteins fold into complex tertiary shapes** that are held in place with a variety of attractive forces. ### Identify the type of interaction depicted here: The image shown includes a diagram representing a section of a protein structure. Described below are the options provided to identify the type of interaction presented in the given diagram. 1. **A) Ion-ion bonds** 2. **B) Disulfide bonds** 3. **C) Hydrogen bonding between functional groups on amino acid residue side chains** 4. **D) Hydrogen bonding between the carbonyl and NH of the backbone of the protein** 5. **E) Hydrophobic attractions (London Dispersion forces) between nonpolar amino acid residue side chains** ### Diagram Interpretation The diagram illustrates a portion of the protein structure emphasizing bonds and interactions within the molecule. Here is a detailed description: - **Hydrophobic Core**: The blue lines in the diagram denote the hydrophobic interactions within the protein core, suggesting the section of the molecule feeling insoluble in water. - **Shown in the Diagram**: The section outlines several molecules (presumably amino acids) interacting within the protein structure, with particular attention to how they hold the 3D shape. Understanding these interactions is crucial for grasping how proteins fold and maintain their tertiary structure, vital for their biological function. **Choose the correct option** based on your understanding of protein structures and the depicted interaction to solidify your understanding of protein chemistry.
Transcribed Image Text:## Understanding Protein Structure and Interactions **Proteins have complex three-dimensional structures.** These polymers are held into these specific shapes with a variety of intermolecular forces, covalent bonds, and ionic bonds. **Proteins fold into complex tertiary shapes** that are held in place with a variety of attractive forces. ### Identify the type of interaction depicted here: The image shown includes a diagram representing a section of a protein structure. Described below are the options provided to identify the type of interaction presented in the given diagram. 1. **A) Ion-ion bonds** 2. **B) Disulfide bonds** 3. **C) Hydrogen bonding between functional groups on amino acid residue side chains** 4. **D) Hydrogen bonding between the carbonyl and NH of the backbone of the protein** 5. **E) Hydrophobic attractions (London Dispersion forces) between nonpolar amino acid residue side chains** ### Diagram Interpretation The diagram illustrates a portion of the protein structure emphasizing bonds and interactions within the molecule. Here is a detailed description: - **Hydrophobic Core**: The blue lines in the diagram denote the hydrophobic interactions within the protein core, suggesting the section of the molecule feeling insoluble in water. - **Shown in the Diagram**: The section outlines several molecules (presumably amino acids) interacting within the protein structure, with particular attention to how they hold the 3D shape. Understanding these interactions is crucial for grasping how proteins fold and maintain their tertiary structure, vital for their biological function. **Choose the correct option** based on your understanding of protein structures and the depicted interaction to solidify your understanding of protein chemistry.
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