Results 1 to 10 of about 30,338 (198)

Heterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusions. [PDF]

open access: goldPLoS ONE, 2013
The expression of heteroligomeric protein complexes for structural studies often requires a special coexpression strategy. The reason is that the solubility and proper folding of each subunit of the complex requires physical association with other ...
Mark A Arbing   +14 more
doaj   +3 more sources

Programming Xenon Diffusion in Maltose Binding Protein

open access: greenSSRN Electronic Journal, 2022
Protein interiors contain void space that can bind small gas molecules. Determination of gas pathways and kinetics in proteins has been an intriguing and challenging task. Here, we combined computational methods and the hyperpolarized xenon-129 chemical exchange saturation transfer (hyper-CEST) NMR technique to investigate xenon (Xe) exchange kinetics ...
Zhuangyu Zhao   +3 more
openalex   +3 more sources

Spectroscopic properties of an engineered maltose binding protein [PDF]

open access: bronzeProtein 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

Accessing a hidden conformation of the maltose binding protein using accelerated molecular dynamics.

open access: goldPLoS Computational Biology, 2011
Periplasmic binding proteins (PBPs) are a large family of molecular transporters that play a key role in nutrient uptake and chemotaxis in Gram-negative bacteria.
Denis Bucher   +3 more
doaj   +2 more sources

A useful epitope tag derived from maltose binding protein [PDF]

open access: hybridProtein 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
openalex   +3 more sources

Further Studies on the Binding of Maltose to the Maltose‐Binding Protein of Escherichia coli [PDF]

open access: bronzeEuropean Journal of Biochemistry, 1976
Extensive binding studies, performed by equilibrium dialysis, suggest that the periplasmic maltosebinding protein of Escherichia coli is homogeneous with respect to its affinity towards maltose. This finding contradicts an earlier conclusion, which was based on insufficient data.
Maxime Schwartz   +3 more
openalex   +4 more sources

Both maltose-binding protein and ATP are required for nucleotide-binding domain closure in the intact maltose ABC transporter [PDF]

open access: greenProceedings of the National Academy of Sciences, 2008
The maltose transporter MalFGK 2 of Escherichia coli is a member of the ATP-binding cassette superfamily. A periplasmic maltose-binding protein (MBP) delivers maltose to MalFGK 2 and stimulates its ATPase activity.
Cédric Orelle   +4 more
openalex   +3 more sources

Protein Modification Employing Non-Canonical Amino Acids to Prepare SUMOylation Detecting Bioconjugates

open access: yesPharmaceutics, 2022
Protein modification with non-canonical amino acids (ncAAs) represents a useful technology to afford homogenous samples of bioconjugates with site-specific modification.
Alexander C. Williard   +10 more
doaj   +1 more source

Competitive interactions of ligands and macromolecular crowders with maltose binding protein. [PDF]

open access: yesPLoS ONE, 2013
Cellular signaling involves a cascade of recognition events occurring in a complex environment with high concentrations of proteins, polysaccharides, and other macromolecules.
Andrew C Miklos   +2 more
doaj   +1 more source

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