Glycine, proline, and serine residues are rarely found in α helices. Explain why this is the case. Why is it the case that glycines are highly conserved in the evolution of proteins?
2. Glycine, proline, and serine residues are rarely found in α helices. Explain why this is the case. Why is it the case that glycines are highly conserved in the evolution of proteins?
Answer :
Because of its asymmetric geometry and steric hindrance caused by its R-connection group's to the amide group's nitrogen, proline destabilises -helices. Additionally, Proline's nitrogen cannot participate in hydrogen bonding since it lacks a hydrogen. The alpha helix bends as a result of proline's destabilising effects.
The smallest amino acid, glycine is distinct in that it lacks a side chain. Glycine can accept bond angles (backbone turns) that are far more severe than those accepted by other amino acids because it lacks a side chain. It consequently has a propensity to bend excessively readily, which deforms the helix
In summary, proline destabilises the helix because of conformational limitations, whereas glycine does it because of its enhanced conformational freedom.
Trending now
This is a popular solution!
Step by step
Solved in 2 steps
