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Chapter 6: Problem 13

Imagine that the dimensions of the alpha helix were such that there were exactly 3.5 amino acids per turn, instead of \(3.6 .\) What would be the consequences for coiled-coil structures?

Short Answer

Expert verified
If there were 3.5 amino acids per turn of the alpha helix instead of 3.6, the helix would be more tightly coiled and potentially less stable due to disruption of hydrogen-bonding. This instability would likely transfer to the coiled-coil structures, making them less stable as well.

Step by step solution

01

Understanding the structure of an Alpha helix

The structure of an alpha helix involves 3.6 residues (amino acids) per turn. It is stabilized by hydrogen bonds between the carbonyl oxygen atom of a residue and the amide hydrogen of the fourth residue away from it. The alpha helix is a right-handed coil.
02

Determine the changes to the alpha helix if there were 3.5 residues per turn instead of 3.6

If there were exactly 3.5 amino acids per turn instead of 3.6, then the helix would have to twist more tightly to accommodate the fewer number of amino acids. This would likely make the alpha helix less stable, due to a disruption of the hydrogen-bonding pattern.
03

Analyzing the consequences on coiled-coil structures

The changes in the alpha helix will have a direct impact on the coiled-coil structures because these structures consist of two or more alpha helices coiled together like the strands of a rope. Since the helices would be more tightly coiled and less stable, the coiled-coil structures would potentially be less stable as well.

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Most popular questions from this chapter

Two polypeptides, \(A\) and \(B\), have similar tertiary structures, but \(A\) normally exists as a monomer, whereas \(\mathrm{B}\) exists as a tetramer, \(\mathrm{B}_{4}\) What differences might be expected in the amino acid composition of A versus B?

It is often observed that Gly residues are conserved in proteins to a greater degree than other amino acids. From what you have learned in this chapter, suggest a reason for this observation.

Poly-L-glutamate adopts an a-helical structure at low pH but becomes a random coil above pH \(5 .\) Explain this behavior.

Discuss the potential contributions to hydrophobic and van der Waals interactions and ionic and hydrogen bonds for the side chains of Asp, Leu, Tyr, and His in a protein.

Pro is the amino acid least commonly found in \(\alpha\) -helices but most commonly found in \(\beta\) -turns, Discuss the reasons for this behavior.
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