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Multiple Choice
Which set of φ and ψ bond angles is best for β-sheet secondary structure?
A
+ Phi (φ) angles & - Psi (ψ) angles.
B
- Phi (φ) angles & + Psi (ψ) angles.
C
+ Phi (φ) angles & + Psi (ψ) angles.
D
- Phi (φ) angles & - Psi (ψ) angles.
Verified step by step guidance
1
Understand the context: In protein secondary structures, the φ (phi) and ψ (psi) angles are the dihedral angles that describe the conformation of the polypeptide chain. These angles are crucial in determining the structure of proteins, such as α-helices and β-sheets.
Recall the Ramachandran plot: This plot is a graphical representation of the φ and ψ angles that are allowed in proteins. Different regions of the plot correspond to different types of secondary structures.
Identify the region for β-sheets: On the Ramachandran plot, β-sheets are typically found in the top left quadrant, which corresponds to negative φ angles and positive ψ angles.
Analyze the options: Compare the given options with the typical φ and ψ angles for β-sheets. The correct set of angles should match the region on the Ramachandran plot where β-sheets are located.
Conclude the best set of angles: Based on the analysis, the set of angles that best represents the β-sheet structure is negative φ angles and positive ψ angles.