Protein stability: experimental data from protein engineering

Abstract

All of molecular recognition, from the binding of substrates by enzymes, information transfer in replicating and processing the genetic information to the folding of proteins, is dominated by non-covalent interactions. Perhaps the most difficult challenge is understanding protein folding because each group in the molecule has to recognize with which ones it has to pair. Protein engineering is providing an experimental entry to determine the magnitude, nature and importance of the various levels of recognition in protein folding. In addition to providing the energetics of specific interactions, fundamental information has been given on the energetics of burial of hydrophobic and hydrophilic solvent-accessible surface areas and their specific roles in stabilizing protein cores and helices.