Recent Advances in Protein Folding
Folding, the formation of the three-dimensional structure, is one of the most important problems in protein chemistry. It is the tertiary structure which determines the biological activity of a protein. The final folded form of a protein is the energetically most favoured conformation. The key information for folding lies in the primary structure. Chemical interactions and disulfide bonding, the activities of some enzymes, are stabilizing factors of the three-dimensional structure. The molecules called "chaperonins" are the recently discovered mediators of protein folding. The production of recombinant proteins in heterologous systems and possible insolubility of the products due to incorrect folding emphasize the importance of understanding the mechanism.
DİNÇTÜRK, Benan (1996) "Recent Advances in Protein Folding," Turkish Journal of Biology: Vol. 20: No. 2, Article 6. Available at: https://journals.tubitak.gov.tr/biology/vol20/iss2/6