Abstract
Many studies have addressed the question why most soluble enzymes are oligomeric (Welch, 1977, Friedman and Beychock, 1979; Jaenicke, 1982). By investigating the kinetics of refolding and reassociation of completely denatured proteins, and also testing the properties of folded but immobilized monomers it has been shown that assembly often modifies the intrinsic catalytic properties of monomers.
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Lane, A.N., Paul, C.H., Kirschner, K. (1984). Conformation Changes in the Assembly of the α2ß2 Complex Of Tryptophan Synthase. In: Ricard, J., Cornish-Bowden, A. (eds) Dynamics of Biochemical Systems. Nato Science Series A: (closed), vol 81. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-5034-8_7
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DOI: https://doi.org/10.1007/978-1-4757-5034-8_7
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