Single amino acid substitutions on the surface of Escherichia coli maltose-binding protein can have a profound impact on the solubility of fusion proteins

Antzeko izenburuak

• Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused.
  nork: Kapust, R. B., et al.
  Argitaratua: (1999)
• Overexpression of bacterio-opsin in Escherichia coli as a water-soluble fusion to maltose binding protein: efficient regeneration of the fusion protein and selective cleavage with trypsin.
  nork: Chen, G. Q., et al.
  Argitaratua: (1996)
• Mutations that alter the equilibrium between open and closed conformations of Escherichia coli maltose-binding protein impede its ability to enhance the solubility of passenger proteins
  nork: Nallamsetty, Sreedevi, et al.
  Argitaratua: (2007)
• Expression of membrane proteins from Mycobacterium tuberculosis in Escherichia coli as fusions with maltose binding protein
  nork: KOREPANOVA, A., et al.
  Argitaratua: (2006)
• Use of gene fusion to study secretion of maltose-binding protein into Escherichia coli periplasm.
  nork: Bassford, P J, et al.
  Argitaratua: (1979)