Results 11 to 20 of about 40,725 (187)
Spectroscopic properties of an engineered maltose binding protein [PDF]
Protein Engineering Design and Selection, 1997 The maltose binding protein (MBP) has been site specifically labelled with a nitrobenzoxadiazole (NBD) group following mutation of a serine to a cysteine residue at position 337. The resulting protein shows a large ligand (maltose or beta-cyclodextrin) dependent increase in its steady-state fluorescence intensity.
Gianfranco Gilardi +4 more
openalex +4 more sources
Stability of Ligand-induced Protein Conformation Influences Affinity in Maltose-binding Protein [PDF]
Journal of Molecular Biology, 2021 ABSTRACTOur understanding of what determines ligand affinity of proteins is poor, even with high-resolution structures available. Both the non-covalent ligand-protein interactions and the relative free energies of available conformations contribute to the affinity of a protein for a ligand.
Marco van den Noort +2 more
openalex +4 more sources
The energetics of structural change in maltose-binding protein [PDF]
Proceedings of the National Academy of Sciences, 2003 High-resolution structures of proteins and their complexes are now appearing in the Research Collaboratory for Structural Bioinformatics (RCSB) database at a tremendous rate. When analyzing the structures of proteins, it is often tempting to try to extract energetic contributions to stability or binding interactions.
David E. Wemmer
openalex +3 more sources
A useful epitope tag derived from maltose binding protein [PDF]
Protein Science, 2021 AbstractMaltose binding protein (MBP) is used in recombinant protein expression as an affinity and solubility tag. The monoclonal antibody B48 binds MBP tightly and has no cross‐reactivity to other proteins in an Escherichia coli lysate. This high level of specificity suggested that MBP contains an epitope that could prove useful as a purification and ...
Marine Lénon +6 more
openaire +2 more sources
Backbone assignment of crystalline E. coli maltose binding protein [PDF]
Biomolecular NMR Assignments, 2021 The E.coli maltose binding protein (MBP) is a 42.5 kDa molecule widely employed in many biotechnology applications. Because of its molecular size, it has become the main model system for the development of solution NMR methods adapted to large biomolecular targets.
Schubeis, Tobias +2 more
openaire +2 more sources
Thermodynamics of maltose binding protein unfolding [PDF]
Protein Science, 1997 AbstractThe maltose binding protein (MBP or MalE) of Escherichia coli is the periplasmic component of the transport system for malto‐oligosaccharides. It is used widely as a carrier protein for the production of recombinant fusion proteins. The melting of recombinant MBP was studied by differential scanning and titration calorimetry and fluorescence ...
V, Novokhatny, K, Ingham
openaire +2 more sources
Engineered Derivatives of Maltose-Binding Protein
, 2012 Maltose-binding protein (MBP), a member of the periplasmic binding protein family of Gram negative bacteria, is a versatile substrate for protein engineering. In common with other periplasmic proteins, it is extremely protease resistant, and it can fold properly in both the cytoplasmic and periplasmic compartments.
Dipak Paul
openalex +4 more sources
Computational analysis of maltose binding protein translocation [PDF]
Philosophical Magazine, 2011 We propose a computational model for the study of maltose binding protein translocation across alpha-hemolysin nanopores. The phenomenological approach simplifies both the pore and the polypeptide chain; however it retains the basic structural protein-like properties of the maltose binding protein by promoting the correct formation of its native key ...
CHINAPPI, MAURO +2 more
openaire +3 more sources
Maltoporins and maltose-binding proteins of Yersinia enterocolitica [PDF]
Journal of General Microbiology, 1993 Two components of the Yersinia enterocolitica maltose transport system, maltoporin (OmpM) and an osmotically shockable periplasmic maltose-binding protein (MBP) were identified. The synthesis of OmpM (apparent Mr 43,000) and transport of maltose into cells of Y. enterocolitica were induced by maltose and maltodextrins.
K, Brzostek, H, Heleszko, J, Hrebenda
openaire +2 more sources
Stubborn contaminants: influence of detergents on the purity of the multidrug ABC transporter BmrA. [PDF]
PLoS ONE, 2014 Despite the growing interest in membrane proteins, their crystallization remains a major challenge. In the course of a crystallographic study on the multidrug ATP-binding cassette transporter BmrA, mass spectral analyses on samples purified with six ...
Benjamin Wiseman +6 more
doaj +1 more source