What Determines Protein Structure?

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Denaturation and renaturation of a protein. High temperatures or various chemical treatments will denature a protein, causing it to lose its shape and hence its ability to function. If the denatured protein remains dissolved, it may renature when the chemical and physical aspects of its environment are restored to normal.

Source: Urry, Lisa A.. Campbell Biology (p. 82). Pearson Education. Kindle Edition.

What Determines Protein Structure? (Campbell Biology)

A polypeptide chain of a given amino acid sequence can be arranged into a three-dimensional shape determined by the interactions responsible for secondary and tertiary structure. This folding normally occurs as the protein is being synthesized in the crowded environment within a cell, aided by other proteins. However, protein structure also depends on the physical and chemical conditions of the protein’s environment. If the pH, salt concentration, temperature, or other aspects of its environment are altered, the weak chemical bonds and interactions within a protein may be destroyed, causing the protein to unravel and lose its native shape, a change called denaturation. Because it is misshapen, the denatured protein is biologically inactive.

Most proteins become denatured if they are transferred from an aqueous environment to a nonpolar solvent, such as ether or chloroform; the polypeptide chain refolds so that its hydrophobic regions face outward toward the solvent. Other denaturation agents include chemicals that disrupt the hydrogen bonds, ionic bonds, and disulfide bridges that maintain a protein’s shape. Denaturation can also result from excessive heat, which agitates the polypeptide chain enough to overpower the weak interactions that stabilize the structure. The white of an egg becomes opaque during cooking because the denatured proteins are insoluble and solidify. This also explains why excessively high fevers can be fatal: Proteins in the blood tend to denature at very high body temperatures.

When a protein in a test-tube solution has been denatured by heat or chemicals, it can sometimes return to its functional shape when the denaturing agent is removed. (Sometimes this is not possible: For example, a fried egg will not become liquefied when placed back into the refrigerator!) We can conclude that the information for building specific shape is intrinsic to the protein’s primary structure; this is often the case for small proteins. The sequence of amino acids determines the protein’s shape—where an α helix can form, where β pleated sheets can exist, where disulfide bridges are located, where ionic bonds can form, and so on.

Source:

Urry, Lisa A.. Campbell Biology. Pearson Education. Kindle Edition. https://www.pearson.com/us/higher-education/series/Campbell-Biology-Series/2244849.html

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