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Secondary Structure of Protein

Secondary structure refers to local folded structures within a polypeptide chain caused by interactions between backbone atoms. The two most common secondary structures are alpha helices and beta pleated sheets. In an alpha helix, hydrogen bonds form between amino acids four positions apart in the chain, pulling it into a helical shape. In a beta pleated sheet, segments of the polypeptide chain line up next to each other, held together by hydrogen bonds between backbone groups while side chains extend above and below the plane. Certain amino acids like proline are more compatible with some structures over others due to their side chain properties.

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121 views

Secondary Structure of Protein

Secondary structure refers to local folded structures within a polypeptide chain caused by interactions between backbone atoms. The two most common secondary structures are alpha helices and beta pleated sheets. In an alpha helix, hydrogen bonds form between amino acids four positions apart in the chain, pulling it into a helical shape. In a beta pleated sheet, segments of the polypeptide chain line up next to each other, held together by hydrogen bonds between backbone groups while side chains extend above and below the plane. Certain amino acids like proline are more compatible with some structures over others due to their side chain properties.

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SahrEmmanuelJr.
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Secondary structure

The next level of protein structure, secondary structure, refers to


local folded structures that form within a polypeptide due to
interactions between atoms of the backbone. (The backbone just
refers to the polypeptide chain apart from the R groups – so all we
mean here is that secondary structure does not involve R group
atoms.) The most common types of secondary structures are the α
helix and the β pleated sheet. Both structures are held in shape by
hydrogen bonds, which form between the carbonyl O of one amino
acid and the amino H of another.
Images showing hydrogen bonding patterns in beta pleated sheets
and alpha helices.
Image credit: OpenStax Biology.

In an α helix, the carbonyl (C=O) of one amino acid is hydrogen


bonded to the amino H (N-H) of an amino acid that is four down the
chain. (E.g., the carbonyl of amino acid 1 would form a hydrogen
bond to the N-H of amino acid 5.) This pattern of bonding pulls the
polypeptide chain into a helical structure that resembles a curled
ribbon, with each turn of the helix containing 3.6 amino acids. The
R groups of the amino acids stick outward from the α helix, where
they are free to interact.

In a β pleated sheet, two or more segments of a polypeptide chain


line up next to each other, forming a sheet-like structure held
together by hydrogen bonds. The hydrogen bonds form between
carbonyl and amino groups of backbone, while the R groups extend
above and below the plane of the sheet^33start superscript, 3, end
superscript. The strands of a β pleated sheet may be parallel,
pointing in the same direction (meaning that their N- and C-termini
match up), or antiparallel, pointing in opposite directions (meaning
that the N-terminus of one strand is positioned next to the C-
terminus of the other).
Certain amino acids are more or less likely to be found in α-helices
or β pleated sheets. For instance, the amino acid proline is
sometimes called a “helix breaker” because its unusual R group
(which bonds to the amino group to form a ring) creates a bend in
the chain and is not compatible with helix formation^44start
superscript, 4, end superscript. Proline is typically found in bends,
unstructured regions between secondary structures. Similarly, amino
acids such as tryptophan, tyrosine, and phenylalanine, which have
large ring structures in their R groups, are often found in β pleated
sheets, perhaps because the β pleated sheet structure provides plenty
of space for the side chains^4

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