In this review, the main concepts of protein folding, as deduced from both theoretical and experimental in vitro studies, are presented. The thermodynamic aspects from Anfinsen's postulate, Levinthal's paradox to the concept of folding funnel as proposed by Wolynes and coworkers are described. Concerning the folding pathway(s), particular attention is brought to bear on the early steps that initiate the process in the light of the results of the fast and even ultrafast techniques presently being used. The role of structural domains as folding units is discussed. Last, from the recent studies, it can be concluded that the main rules deduced from the in vitro folding studies are valid for the folding of a nascent polypeptide chain in vivo.