Just want to point out that the “hydrophobic effect” is one of , if not the, most important contributors to protein folding. read more
Protein folding is influenced almost 100% by H2O interactions. Remember, hydrophobic segments of proteins are typically internal segments of proteins, while hydrophilic segments remain on the outside, interacting with water molecules. Therefore, it affects mainly the tertiary and quaternary structures. read more
Water is therefore fundamental in protein folding because of its role in defining hydrophobic attractions. The hydrophobic “collapse” of the protein is necessarily accompanied, and guided, by hydrogen-bond formation between favorable functional groups [12]. read more
Protein Folding. Proteins are folded and held together by several forms of molecular interactions. The molecular interactions include the thermodynamic stability of the complex, the hydrophobic interactions and the disulfide bonds formed in the proteins. The figure below (figure 3) is an example of protein folding. read more