Why do common folding patterns appear in proteins that exhibitvery different primary structures?
The carbonyl and amino groups of the amino-acid residues at theN- and C-termini of proteins form regular patterns of hydrogenbonds that define α-helix and β-sheet shapes.
The carbonyl and amide groups of the polypeptide backbone formregular patterns of hydrogen bonds that define α-helix and β-sheetshapes.
The carbonyl and amino groups of glutamate and glutamine,respectively, form regular patterns of ionic bonds that defineα-helix and β-sheet shapes.
The carboxyl and amino groups of the amino-acid residues at theN-and C-termini of proteins form regular patterns of ionic bondsthat define α-helix and β-sheet shapes.
The carbonyl and amide groups of the amino-acid sidechains formregular patterns of hydrogen bonds that define α-helix and β-sheetshapes.
