Proline isomerization and the slow folding reactions of the α subunit of tryptophan synthase from Escherichia coli
Ziegelhoeffer A.; De Jong J.W.; Ferrari R.; Turi Nagy L.
Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology 913(2): 179-184
1987
DOI: 10.1016/0167-4838(87)90328-1
Accession: 061943242
Previous studies on the refolding of the alpha subunit of tryptophan synthase from Escherichia coli assigned two slow refolding phases to rate-limiting isomerizations of two 'essential' proline residues, one in each of the two domains of the protein (Matthews, C.R., Crisanti, M.M., Manz, J.T. and Gepner, G.L. (1983) Biochemistry 22, 1445-1452).