Question

When proteins are subjected to heat and undergo denaturation so that the tertiary structure is altered, what happens to the R groups in the interior and on the surface of the molecule? why is this important?

Answer 1

Proteins in their native form are in a thermodynamically stable state, usually with hydrophobic amino acids toward the interior of the protein and hydrophilic amino acids on the exterior of the protein. Heating the protein can disrupt interactions between the R groups of the amino acids, causing it to unfold.

Once a protein unfolds, the R groups of the amino acids will be interacting with their environment, which may or may not be thermodynamically favorable. Once the protein is cooled, it will refold and the amino acids of the protein will try to interact with each other again. This refolding will most likely result in a misfolded protein that no longer has its original function.