‘Morphs’ (MRFs): metal-reversible folding domains for differential IgG binding
Open Access
- 31 December 2001
- journal article
- research article
- Published by Elsevier
- Vol. 8 (12) , 1221-1229
- https://doi.org/10.1016/s1074-5521(01)00088-6
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Protein engineering of an IgG-binding domain allows milder elution conditions during affinity chromatographyJournal of Biotechnology, 2000
- Escherichia coli maltose‐binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fusedProtein Science, 1999
- A chemical-detecting system based on a cross-reactive optical sensor arrayNature, 1996
- Expression of correctly folded proteins in Escherichia coliCurrent Opinion in Biotechnology, 1996
- Engineered bacterial receptors in immunologyCurrent Opinion in Immunology, 1993
- A Novel, Highly Stable Fold of the Immunoglobulin Binding Domain of Streptococcal Protein GScience, 1991
- The role of internal packing interactions in determining the structure and stability of a proteinJournal of Molecular Biology, 1991
- Thiol‐directed immobilization of recombinant IgG‐binding receptorsEuropean Journal of Biochemistry, 1989
- Purification of streptococcal protein g expressed byEscherichia coli by high performance liquid affinity chromatography using immobilized immunoglobulin G and albuminBiomedical Chromatography, 1987
- Fluorescence Spectroscopy of ProteinsScience, 1968