Structural Levels of Proteins and Denaturation

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25 Terms

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<p>Primary protein</p>

Primary protein

Is a sequence of a chain of amino acids

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Secondary protein

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Occurs when the sequence of amino acids are linked by hydrogen bonds

The polypeptide chains are folded regularly

Hydrogen bonding causes protein chains to fold and align to produce orderly patterns

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The 2 prominent structure of secondary proteins are

  • Alpha helix

  • Beta pleated sheet

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Alpha helix

Single protein chain twisted to resemble a coiled helical spring

<p>Single protein chain twisted to resemble a coiled helical spring</p>
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Alpha helix is stabilized by

hydrogen bonds between the electropositive nitrogen atom of a peptide linkage and the electronegative carbonyl atom of the 4th amino acid on the amino terminal side of the peptide bond

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Left alpha helix

The n-terminal is on the left side

<p>The n-terminal is on the left side</p>
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Right alpha helix

The n-terminal is on the right side

<p>The n-terminal is on the right side</p>
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Beta pleated sheet

The polypeptide chain is extended into a zigzag arrangement

Polypeptide chains are arranged side by side in the form of pleats/sheets

The adjacent chains can be parallel or antiparallel

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What stabilize the beta pleated sheet

Hydrogen bonds are formed between adjacent segments of polypeptide chains

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Parallel beta sheet

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Antiparallel beta sheet

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Tertiary protein

Occurs when certain attractions between alpha helices and pleasted sheets

It is the overall three-dimensional arrangement of all atoms in a protein

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Forces involve to stabilize the tertiary and quaternary protein structure

  • Hydrophobic interactions (nonpolar groups cluster inside)

  • Hydrogen bonds (between polar groups)

  • Disulfide bridges (-S-S-) (covalent bonds between cysteine residues)

  • Ionic bonds (between charged side chains)

<ul><li><p class=""><strong>Hydrophobic interactions</strong> (nonpolar groups cluster inside)</p></li><li><p class=""><strong>Hydrogen bonds</strong> (between polar groups)</p></li><li><p class=""><strong>Disulfide bridges (-S-S-)</strong> (covalent bonds between cysteine residues)</p></li><li><p class=""><strong>Ionic bonds</strong> (between charged side chains)</p></li></ul><p></p>
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Quaternary protein

Is a protein consisting of more than one amino acid chain

The arrangement of two or more polypeptide chains (subunits) into a functional protein.

  • Example:

    • Hemoglobin (contains 4 subunits)

    • Collagen (triple-helix structure)

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Denaturation

Is the structural changes in proteins that can cause loss of function due to:

  • heat

  • extreme pH

  • organic solvents

  • solutes

<p>Is the structural changes in proteins that can cause loss of function due to:</p><ul><li><p>heat </p></li><li><p>extreme pH</p></li><li><p>organic solvents</p></li><li><p>solutes</p></li></ul><p></p>
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Hemoglobin

Transport protein that carries oxygen in the blood

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Collagen

  • Fibrous protein in connective tissue

  • Found in tendons, bone, cartilage, and blood vessels

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Ferritin

Protein that stores iron in the liver

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Actin and Myosin

Proteins that control muscle contraction

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Keratin

fibrous protein in hair, skin, and nail

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Myoglobin

Protein that stores oxygen in tissues

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Insulin

  • Protein hormone synthesized in the pancreas

  • Controls blood glucose levels

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Types of Denaturation

  • Flocculation

  • Coagulation

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Flocculation

clumping together of the dispersed chain of the denatured protein

this denaturation is reversible

<p>clumping together of the dispersed chain of the denatured protein</p><p>this denaturation is reversible</p>
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Coagulation

Occurs when the flocculated protein is heated further. The clumped chains become insoluble not only at its isoelectric pH but also over the entire pH range

this denaturation is irreversible