Energetics of Protein Folding and Significance of Intermediates

Protein folding has now been accepted to be a self assembly process with favorable environmental parameters. The process involves free energy change from unfolded to folded state due to various interactions (ionic, covalent, and hydrogen bonds, hydrophobic interactions) leading to lowest energy state of native three-dimensional structure. From past decades, researchers are trying to predict native tertiary structure of the protein from amino acid sequence using folding energetics parameters. Further, efforts are also being made to understand protein–protein and protein–ligand interactions based on folding energetics studies.