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Which of the conformations illustrated above (a or b) is more likely PrPc (the normal cellular form of PrP) and which is more likely PrPSc (the pathogenic form of PrP)?  Why?

Which of the conformations illustrated above (a or b) is more likely PrPc (the normal cellular form of PrP) and which is more likely PrPSc (the pathogenic form of PrP)?  Why?

Human Anatomy & Physiology (11th Edition)
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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Which of the conformations illustrated above (a or b) is more likely PrPc (the normal cellular form of PrP) and which is more likely PrPSc (the pathogenic form of PrP)?  Why?

This image depicts two ribbon diagrams illustrating different structural elements of proteins. **Diagram (a)**: 1. **Description**: The diagram displays a combination of alpha-helices (depicted as coiled ribbons) and loops (shown as thin lines). 2. **Color Coding**: - The alpha-helices are colored red, green, and white, indicating different segments of the helix or possibly highlighting variations in the amino acid sequence or secondary structure. - The loops connecting the helices are colored yellow, indicating flexible regions between the more rigid helices. 3. **Structure Detailing**: - The helices are coiled, showcasing the characteristic helical structure formed by hydrogen bonds between the backbone amides of amino acids. - These helices are connected by short loop regions which allow for the transition from one helix to another. **Diagram (b)**: 1. **Description**: This diagram shows a mixed structure composed of both beta-strands and alpha-helix. 2. **Color Coding**: - The beta-strands are colored green and form part of beta-sheets. - The alpha-helices are red, distinct from the beta-strands. - The loops connecting these regions are depicted as white and yellow thin lines. 3. **Structure Detailing**: - The beta-strands are represented by arrows pointing in the direction of the polypeptide chain, indicative of their parallel or anti-parallel orientation in a beta-sheet. - These strands form the edges of the protein structure, highlighting the sheet-like arrangement. - The loops and turns, shown as flexible regions, connect different beta-strands and the helical region, allowing the protein to fold into a specific three-dimensional structure. These diagrams collectively illustrate the complexity and diversity of protein secondary structure. The alpha-helix and beta-sheet are fundamental elements of protein architecture, enabling the formation of the intricate tertiary structures required for biological function. Understanding these structures is crucial for studying protein function, stability, and interactions.
Transcribed Image Text:This image depicts two ribbon diagrams illustrating different structural elements of proteins. **Diagram (a)**: 1. **Description**: The diagram displays a combination of alpha-helices (depicted as coiled ribbons) and loops (shown as thin lines). 2. **Color Coding**: - The alpha-helices are colored red, green, and white, indicating different segments of the helix or possibly highlighting variations in the amino acid sequence or secondary structure. - The loops connecting the helices are colored yellow, indicating flexible regions between the more rigid helices. 3. **Structure Detailing**: - The helices are coiled, showcasing the characteristic helical structure formed by hydrogen bonds between the backbone amides of amino acids. - These helices are connected by short loop regions which allow for the transition from one helix to another. **Diagram (b)**: 1. **Description**: This diagram shows a mixed structure composed of both beta-strands and alpha-helix. 2. **Color Coding**: - The beta-strands are colored green and form part of beta-sheets. - The alpha-helices are red, distinct from the beta-strands. - The loops connecting these regions are depicted as white and yellow thin lines. 3. **Structure Detailing**: - The beta-strands are represented by arrows pointing in the direction of the polypeptide chain, indicative of their parallel or anti-parallel orientation in a beta-sheet. - These strands form the edges of the protein structure, highlighting the sheet-like arrangement. - The loops and turns, shown as flexible regions, connect different beta-strands and the helical region, allowing the protein to fold into a specific three-dimensional structure. These diagrams collectively illustrate the complexity and diversity of protein secondary structure. The alpha-helix and beta-sheet are fundamental elements of protein architecture, enabling the formation of the intricate tertiary structures required for biological function. Understanding these structures is crucial for studying protein function, stability, and interactions.
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