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 th
e light of the results of the fast and even ultrafast techniques prese
ntly being used. The role of structural domains as folding units is di
scussed. Last, from the recent studies, it can be concluded that the m
ain rules deduced from the in vitro folding studies are valid for the
folding of a nascent polypeptide chain in vivo.