The most important contribution to the stability of a protein conformation appears to be the
entropy increase from the decrease in ordered water molecules forming a solvent shell around it
maximum entropy increase from ionic interactions between the ionized amino acids in a protein
sum of free energies of formation of many weak interactions between its polar amino acids and surrounding water molecules
sum of free energies of formation of many weak interactions among the hundreds of amino acids in a protein
Several weak electrostatic attraction exist between the amino acid units of protein. These interactions lower the free energy to a very great extent.