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The secondary structure of a protein is a property of an individual polypeptide chain. It is the conformation that the chain of amino acids acquires. The major types of secondary structure are: coil (an alpha helix) sheet (a beta pleated sheet) turn (a tight bend made up of four amino acids, especially including proline, which forms a rigid kink, and glycine, which has a tiny side-chain) There are also more or less amorphous regions, referred to by such terms as loops and random coils. Secondary structures are held in place by hydrogen bonding. The secondary structure of a chain is hierarchically between the primary structure (the amino acid sequence) and the tertiary structure (higher-level folding, stabilized by charge, hydrophobic interaction, and by covalent sulfur-sulfur bridges).

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15y ago
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6y ago

HYDROGEN BONDS
Hydrogen bonds between the side chains ( not R groups ) of amino acids.

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11y ago

Crosslinks incorporated by the peptides lead to conformationally stabilization of helical folds.

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12y ago

The many bondings of the amino acid R groups. Hydrophyllic, hydrophobic, acisid, basic and disulphide bridges.

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11y ago

hydrogen bonds

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14y ago

hydrogen bonds

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13y ago

regularly spaced hydrogen bondings

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13y ago

Hydrogen bonds.

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Q: What types of chemical bonds are involved in maintaining the secondary structure of a protein?
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