Home
  >  
Section 62
  >  
Chapter 61,944

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

Download citation:  
Text
  |  
BibTeX
  |  
RIS

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).

PDF emailed within 0-6 h: $19.90