THE ROLE OF AB-INITIO QUANTUM-CHEMISTRY AND OTHER THEORETICAL METHODS IN THE UNDERSTANDING OF PROTEIN CONFORMATIONS

For the determination of the conformation of a protein on the basis of its amino acid sequence extensive ab initio quantum chemical calculations on oligopeptides are first briefly described. From these computations determination of the secondary structure of polypeptide segments is expected. To treat the difficult, but very important, problem of protein folding (tertiary structure), the proper application of a neuron network is outlined. To determine the entropy contribution, solvent and substrate effects in enzyme conformations, most probably again neuron networks, can be applied. Finally, for the time average of the very numerous nearly degenerate conformational minima of a protein the idea of an ''effective conformation'' is introduced. To determine this a combination of molecular dynamics simulations and sophisticated statistical physical methods is proposed.