Abstract
Oligomeric proteins have been created as an evolutionary solution to fulfill specific cellular tasks, trading off functional and molecular requirements such as domain organization, molecular economy, minimization of the size of structural genes, reducing the costs for elimination of misfolded polypeptide chains, cooperativity, tight control, etc. Oligomers are also a challenging experimental object to test our concepts of the sequence-structure-energy-function relationships in proteins. In this paper, we briefly discuss the evolutionary aspects of the appearance of oligomers, and present with a few selected examples the current state of affairs in understanding the folding of small oligomeric proteins.