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Artificial Allosteric Control of Maltose Binding Protein
Physical Review Letters, 2005We demonstrate the allosteric control of a protein based on mechanical tension. When substrate binding is accompanied by a significant change of conformation of the protein, a mechanical tension favoring one or the other conformation will alter the binding affinity for the substrate.
Jeanne Perry +5 more
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Ligand Binding Mechanics of Maltose Binding Protein
Journal of Molecular Biology, 2009In the past decade, single-molecule force spectroscopy has provided new insights into the key interactions stabilizing folded proteins. A few recent studies probing the effects of ligand binding on mechanical protein stability have come to quite different conclusions.
Morten Bertz +2 more
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Immune responses to hybrid maltose-binding proteins
Vaccine, 1993The Escherichia coli maltose-binding protein is a highly versatile carrier protein allowing the construction of genetically engineered hybrid proteins. It accepts large fusions to both C- and N-termini as well as the insertion of shorter peptides at 'permissive sites' within the continuity of the protein.
Pierre Martineau +6 more
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Journal of Molecular Biology, 1996
Small-angle X-ray scattering experiments were carried out for the maltose-, glucose/galactose- and ribose-binding proteins of Gram negative bacteria. All were shown to be monomers that decrease in radius of gyration on ligand binding.
B. Shilton +3 more
semanticscholar +1 more source
Small-angle X-ray scattering experiments were carried out for the maltose-, glucose/galactose- and ribose-binding proteins of Gram negative bacteria. All were shown to be monomers that decrease in radius of gyration on ligand binding.
B. Shilton +3 more
semanticscholar +1 more source
Protein Expression and Purification, 1998
When the mammalian aspartic proteinases, procathepsin D or pepsinogen, are expressed in Escherichia coli both accumulate in inclusion bodies. While pepsinogen is efficiently refolded in vitro, recovery of procathepsin D is limited by insolubility.
D. Sachdev, John M. Chirgwin
semanticscholar +1 more source
When the mammalian aspartic proteinases, procathepsin D or pepsinogen, are expressed in Escherichia coli both accumulate in inclusion bodies. While pepsinogen is efficiently refolded in vitro, recovery of procathepsin D is limited by insolubility.
D. Sachdev, John M. Chirgwin
semanticscholar +1 more source
Strategy for purifying maltose binding protein fusion proteins by affinity precipitation.
Journal of Chromatography A, 2008The maltose binding protein (MBP) affinity tag has been extensively used for protein purification. A commercial grade cationic starch could precipitate MBP or an MBP-tagged protein quantitatively by simultaneous addition of 10% (w/v) polyethylene glycol (PEG) and 50 mM calcium chloride.
Smita Raghava +4 more
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Engineering the Maltose Binding Protein for Reagentless Fluorescence Sensing
Analytical Chemistry, 1994This paper describes a mutant of the maltose binding protein (MBP) in which the serine residue at position 337 is replaced by a cysteine residue using site-directed mutagenesis. The mutant MBP has an approximately 2-fold lower affinity for maltose, and the cysteine residue can be modified with 4-[N-(2-(iodoacetoxy)ethyl)-N-methylamino]-7-nitrobenz-2 ...
Gianfranco Gilardi +3 more
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Maltose-binding protein: a versatile platform for prototyping biosensing
Current Opinion in Biotechnology, 2006The bacterial periplasmic-binding protein (PBP) superfamily members, in particular the maltose-binding protein, have been used extensively to prototype a variety of biosensing platforms. Although quite diverse at the primary sequence level, this protein superfamily retains the same basic two-domain structure, and upon binding a recognized ligand almost
Jeffrey R. Deschamps, Igor L. Medintz
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Mechanical Unfoldons as Building Blocks of Maltose-binding Protein
Journal of Molecular Biology, 2008Identifying independently folding cores or substructures is important for understanding and assaying the structure, function and assembly of large proteins. Here, we suggest mechanical stability as a criterion to identify building blocks of the 366 amino acid maltose-binding protein (MBP). We find that MBP, when pulled at its termini, unfolds via three
Morten Bertz +2 more
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Expression and Purification of Maltose‐Binding Protein Fusions
Current Protocols in Molecular Biology, 1994AbstractThis unit describes the procedure for subcloning the sequence encoding the protein of interest into an maltose‐binding protein (MBP) vector, and expressing and purifying the fusion protein from the cytoplasm. MBP vectors include a sequence that encodes the four‐amino‐acid recognition site for the specific protease factor Xa.
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