ABSTRACT
It has almost become a truism for more than a generation of biochemists that the acquisition of the native functional state of proteins is a spontaneous and autonomous process depending solely on the amino acid sequence and its (quasi-) physiological environment. As has been demonstrated by Anson and his colleagues, who pioneered the field long before the three-dimensional structure of a single protein was known, the natural cellular environment can be mimicked by wellchosen buffers. Based on this discovery, the time course of protein folding and association has been investigated in great detail leading to plausible models describing sequential and multiple pathways of protein self-organization.
