Molecular analysis of cyclic α-maltosyl-(1→6)-maltose binding protein in the bacterial metabolic pathway. [PDF]
PLoS ONE, 2020 Cyclic α-maltosyl-(1→6)-maltose (CMM) is a cyclic glucotetrasaccharide with alternating α-1,4 and α-1,6 linkages. Here, we report functional and structural analyses on CMM-binding protein (CMMBP), which is a substrate-binding protein (SBP) of an ABC ...
Masaki Kohno +6 more
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Competitive interactions of ligands and macromolecular crowders with maltose binding protein. [PDF]
PLoS 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
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Programming xenon diffusion in maltose-binding protein. [PDF]
Biophys J, 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 ...
Zhao Z, Rudman NA, He J, Dmochowski IJ.
europepmc +3 more sources
A useful epitope tag derived from maltose binding protein. [PDF]
Protein Sci, 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 ...
Lénon M +6 more
europepmc +4 more sources
Purity of maltose-binding protein – Recombinant streptavidin expressed in Escherichia coli BL21 (pD861-MBP: 327892) [PDF]
Journal of Advanced Pharmaceutical Technology & Research, 2022 Nearly 95% of streptavidin which is expressed in Escherichia coli found as an inclusion body. Protein expressed in an inclusion body form requires further steps for the folding process related to its purification.
Toto Subroto +5 more
doaj +2 more sources
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
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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
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Accessing a hidden conformation of the maltose binding protein using accelerated molecular dynamics.
PLoS 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
Maltose-Binding Protein (MBP), a Secretion-Enhancing Tag for Mammalian Protein Expression Systems. [PDF]
PLoS ONE, 2016 Recombinant proteins are commonly expressed in eukaryotic expression systems to ensure the formation of disulfide bridges and proper glycosylation. Although many proteins can be expressed easily, some proteins, sub-domains, and mutant protein versions ...
Raphael Reuten +7 more
doaj +2 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