Understanding Alpha Helices Classifications

  • Thread starter icedoverfire
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In summary: This can be seen on an atomic level, with 0's representing the h-bonded atoms. In summary, alpha helices are classified by their number of residues per turn and the number of atoms in between hydrogen bonds, with the N and N+4th residues being hydrogen bonded in both the 3.613 and 310 helices.
  • #1
icedoverfire
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Hi folks,

I'm confused about classifying alpha helices. I don't understand how a 3.613 and a 310 helix differentiate... Well, I know that a 3.613 helix has 3.6 residues per turn and 13 atoms in between each hydrogen bond (I think)?
Likewise a 310 helix has 3 residues per turn and 10 atoms in between each hydrogen bond (I think)?
But what confuses me is that despite these classifications in both helices the N and N+4th residues are hydrogen bonded? So in a 3.613 helix 13 atoms span the distance between hydrogen bonds but the 1st and 5th residues (for example) would be linked via hydrogen bond (with 13 atoms in between the hydrogen bond)?

so it'd look something like this, on an atomic level (0's are the h-bonded atoms)?

0-1-2-3-4-5-6-7-8-9-10-11-12-13-0

Am I reading too deeply into this?

Thanks,

-ice
 
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  • #2
No, you are not reading too deeply into this. Alpha helices are classified by the number of residues per turn and the number of atoms in between the hydrogen bonds. The 3.613 helix has 3.6 residues per turn and 13 atoms in between the hydrogen bonds, while the 310 helix has 3 residues per turn and 10 atoms in between the hydrogen bonds. The N and N+4th residues in both helices are hydrogen bonded, with the difference being the number of atoms that span the distance between the two hydrogen bonds.
 
  • #3
breaker

Hello icebreaker,

Thank you for your question about alpha helix classifications. It is normal to feel confused about these classifications, as they can be quite technical and nuanced. Let me try to provide some clarification for you.

First, you are correct in your understanding of the differences between a 3.613 and a 310 helix. The numbers represent the number of residues per turn, and the number of atoms between each hydrogen bond.

In terms of the N and N+4th residues being hydrogen bonded, this is a general trend seen in most alpha helices. The N and N+4th residues are typically involved in hydrogen bonding, regardless of the specific classification of the helix. This is because the 4th residue is directly across from the first residue in the helix, and therefore is in close proximity for hydrogen bonding.

Your atomic level representation is also correct. The 0's represent the hydrogen bonded atoms, and the numbers represent the number of atoms between each hydrogen bond.

Overall, it is important to understand the general trends and differences between alpha helix classifications, but it is also important to remember that there can be variations and exceptions within these classifications. So, you are not reading too deeply into this, but it is also important to keep in mind that these are just general guidelines.

I hope this helps to clarify things for you. If you have any further questions, please don't hesitate to ask.

Best,
 

1. What is the primary structure of an alpha helix?

The primary structure of an alpha helix is a linear sequence of amino acids connected by peptide bonds. It is the first level of protein structure and determines the order of the amino acids in the polypeptide chain.

2. How is the secondary structure of an alpha helix determined?

The secondary structure of an alpha helix is determined by the hydrogen bonding between the carbonyl group of one amino acid and the amino group of another amino acid four residues down the chain. This creates a helical structure with a repeating pattern of hydrogen bonds.

3. What are the different classifications of alpha helices?

The different classifications of alpha helices include regular and irregular, based on the spacing between the amino acids in the helix. Other classifications include right-handed and left-handed, based on the direction of the helix rotation, and parallel and antiparallel, based on the orientation of the peptide bonds in the helix.

4. How does the amino acid sequence affect the stability of an alpha helix?

The amino acid sequence plays a crucial role in the stability of an alpha helix. Certain amino acids, such as alanine and glutamate, have a high propensity to form alpha helices, while others, such as proline and glycine, destabilize the helix structure. The presence of bulky or charged amino acids can also disrupt the hydrogen bonding and destabilize the helix.

5. Can alpha helices have functional roles in proteins?

Yes, alpha helices can have functional roles in proteins. They can act as structural elements, providing rigidity and stability to the protein, or they can be involved in protein-protein interactions. Alpha helices can also serve as membrane-spanning regions in integral membrane proteins or as recognition sites for binding specific molecules or ions.

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