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
- 21 December 2007
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 364 (3) , 639-644
- https://doi.org/10.1016/j.bbrc.2007.10.060
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Accumulation of partly folded states in the equilibrium unfolding of ervatamin A: Spectroscopic description of the native, intermediate, and unfolded statesBiochimie, 2007
- The acidity of protein fusion partners predominantly determines the efficacy to improve the solubility of the target proteins expressed in Escherichia coliJournal of Biotechnology, 2007
- Enhancement of soluble protein expression through the use of fusion tagsCurrent Opinion in Biotechnology, 2006
- Gateway vectors for the production of combinatorially‐tagged His6‐MBP fusion proteins in the cytoplasm and periplasm of Escherichia coliProtein Science, 2005
- Escherichia coli fusion carrier proteins act as solubilizing agents for recombinant uncoupling protein 1 through interactions with GroELBiochemical and Biophysical Research Communications, 2005
- Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partnersProtein Expression and Purification, 2005
- Making the most of affinity tagsTrends in Biotechnology, 2005
- Production of soluble mammalian proteins in Escherichia coli: identification of protein features that correlate with successful expressionBMC Biotechnology, 2004
- Mechanisms for GroEL/GroES-mediated Folding of a Large 86-kDa Fusion Polypeptide in VitroJournal of Biological Chemistry, 1999
- High-Level Expression of Soluble Protein inEscherichia coliUsing a His6-Tag and Maltose-Binding-Protein Double-Affinity Fusion SystemProtein Expression and Purification, 1997