Conformation Changes in the Assembly of the α2ß2 Complex Of Tryptophan Synthase
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.
KeywordsPyridoxal Phosphate Partial Assembly Isomerization Process Carbon Proton Thermodynamic Dissociation Constant
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- Bernasconi, C. (1976) “Relaxation kinetics”, Academic Press, New-York.Google Scholar
- Lane, A.N. and Kirschner, K. (1984) ENBO J. 4, 279–287.Google Scholar
- Levitzki, A. (1975) in “Subunits Enzymes, Biochemistry and Function” Ebner, K.E. ed. pp. 1–41., Marcel Dekker, New-York.Google Scholar
- Miles, E.W. (1979) Advanc. Enzymol. Relat. Areas Mol. Biol. 49, 127–136.Google Scholar