Respuesta :
The reason a proline residue in the middle of an α helix is predicted to be destabilizing to the helical structure is Pro does not have the α−NH group that acts as a stabilizing H-bond donor in the middle of the helix and Pro is not able to adopt the ideal ϕ and ψ angles for an α -helix.
Proline residues are important in the folding, misfolding, and aggregation of proteins [1, 2, 3]. They are essential for achieving proteins' functional state [4]. Prolines are also involved in domain switching [5,6] and the formation of amyloid fibrils from protein aggregation [7,8,9].
Proline residues are abundant in -helices, where they frequently serve crucial roles in the structure and function of the protein. This is evident now that there are over 30,000 protein structures in the Protein Data Bank. Due to its asymmetric geometry and reversible R-group link to the nitrogen of the amide group, proline additionally hinders steric flow and destabilizes -helices. Additionally, Proline's nitrogen cannot participate in hydrogen bonding since it lacks hydrogen.
The complete question is:
Give two reasons to explain why a proline residue in the middle of an α-helix is predicted to be destabilizing to the helical structure.
Chek all that apply.
-Pro does not have the α−NH group that acts as a stabilizing H-bond donor in the middle of the helix.
-Pro is not able to adopt the ideal ϕ and ψ angles for an α -helix.
-Pro is nonpolar amino acid that destabilizes polar core of the protein.
-Pro is nonpolar amino acid that does not connect turns of the α-helix.
-Insertion of Pro gives an exceptional conformational rigidity to the protein chain chain.
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