Results 161 to 170 of about 40,725 (187)
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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.
Brian, Choi +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, Matthias, Rief
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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.
D, O'Callaghan +6 more
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Purification of Proteins Fused to Maltose-Binding Protein
2010Maltose-binding protein (MBP) is one of the most popular fusion partners being used for producing recombinant proteins in bacterial cells. MBP allows one to use a simple capture affinity step on amylose-agarose columns, resulting in a protein that is often 70-90% pure.
Mario, Lebendiker, Tsafi, Danieli
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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 ...
G, Gilardi +3 more
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Protein Purification with C-Terminal Fusion of Maltose Binding Protein
Protein Expression and Purification, 1998For affinity-chromatography-based purification of proteins that are prone to abnormal termination of translation or that may not be modified at their N-termini, affinity tags are needed which can be fused to the C-terminus. In this publication we describe that maltose binding protein (MBP) fused to the C-terminus of the plant photoreceptor phytochrome ...
L, Hennig, E, Schäfer
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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
Igor L, Medintz, Jeffrey R, Deschamps
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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, Matthias, Rief
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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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Membrane Protein Topology Determination by Proteolysis of Maltose Binding Protein Fusions
Analytical Biochemistry, 1993A method is presented for determining the topology of Escherichia coli inner membrane proteins that is based on proteolysis of fusion proteins between maltose binding protein (MBP) and the membrane protein of interest. Fusion proteins are constructed wherein the MBP domain is fused upstream of the membrane protein domain.
K W, Miller +3 more
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