Folding of Macromolecules
In the case of protein folding, the hydrophobic effect is important to understand the structure of proteins that have hydrophobic amino acids, such as alanine, valine, leucine, isoleucine, phenylalanine, tryptophan and methionine clustered together within the protein. Structures of water-soluble proteins have a hydrophobic core in which side chains are buried from water, which stabilizes the folded state, and charged and polar side chains are situated on the solvent-exposed surface where they interact with surrounding water molecules. Minimizing the number of hydrophobic side chains exposed to water is the principal driving force behind the folding process, although formation of hydrogen bonds within the protein also stabilizes protein structure.
The energetics of DNA tertiary structure assembly were determined to be driven by the hydrophobic effect, in addition to Watson-Crick base pairing (which is responsible for sequence selectivity) and a significant contribution from stacking interactions between the aromatic bases.
Read more about this topic: Hydrophobic Effect
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