A protein requires its own three-dimensional structure for its biological activity. If a chemical agent is added, the biological activity is lost, and the three dimensional structure is destroyed to become a random coil state. But when the chemical agent is removed, the biological activity is recovered, implying that the random coil state turns back into the original complex structure spontaneously. This is an astonishing event. The Physical Foundation of Protein Architecture is intended to solve this mystery from the physicochemical basis by elucidating the mechanism of various processes in protein folding. The main features of protein folding are shown to be described by the island model with long range hydrophobic interaction which is capable of finding the specific residue, and the lampshade criterion for disulfide bonding. Various proteins with known structure are refolded, with the purpose of uncovering the mechanism of protein folding. In addition, ab initio method for predicting protein structure from its amino acid sequence is proposed.
Generalities: helix-coil transition in polypeptide; some aspects of protein folding. Mechanism of protein folding: island model; a-helical proteins; lysozyme and phospholipase; bovine pancreatic trypsin inhibitor; flavodoxin and thioredoxin; ferredoxin. Folding of a protein of unknown structure: ab initio method of prediction of protein structure; search for the conformation of minimum energy. Topics related to protein structures: phase transition; module; molecular chaperones; membrane proteins; structure prediction based on protein data.