Why do common folding patterns appear in proteins that exhibit very different primary structures? The carbonyl and...

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Biology

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 Î±-helix and Î²-sheet shapes.
The carbonyl and amide groups of the polypeptide backbone formregular patterns of hydrogen bonds that define Î±-helix and Î²-sheetshapes.
The carbonyl and amino groups of glutamate and glutamine,respectively, form regular patterns of ionic bonds that defineÎ±-helix and Î²-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 Î±-helix and Î²-sheet shapes.
The carbonyl and amide groups of the amino-acid sidechains formregular patterns of hydrogen bonds that define Î±-helix and Î²-sheetshapes.

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The second option is the correct answer ie The carbonyl and amide groups of the polypeptide backbone form regular patterns of hydrogen bonds that define helix and sheet shapes See Answer

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