Results 291 to 300 of about 940,374 (326)

Analysis of the sensitization activity of Moringa oleifera leaves protein. [PDF]

Front Nutr
Lu J, Liu X, Li W, Xi C, Feng D, Song S.
europepmc   +1 more source

Purification of proteins fused to maltose-binding protein. [PDF]

Methods in molecular biology, 2011
Maltose-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.
M. Lebendiker, T. Danieli
semanticscholar   +4 more sources

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Artificial Allosteric Control of Maltose Binding Protein

Physical Review Letters, 2005
We 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, Stephan Canale, Giovanni Zocchi, Sum Chan, Yim Wu, Brian Choi   +5 more
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Ligand Binding Mechanics of Maltose Binding Protein

Journal of Molecular Biology, 2009
In 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, Matthias Rief   +2 more
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Immune responses to hybrid maltose-binding proteins

Vaccine, 1993
The 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, Alain Charbit, Claude Leclerc, Maurice Hofnung, David O'Callaghan, Catherine Fayolle, Jean-Gérard Guillet   +6 more
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Engineering the Maltose Binding Protein for Reagentless Fluorescence Sensing

Analytical Chemistry, 1994
This 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, Li Qing. Zhou, Linda. Hibbert, Anthony E. G. Cass   +3 more
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Maltose-binding protein: a versatile platform for prototyping biosensing

Current Opinion in Biotechnology, 2006
The 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, 2008
Identifying 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, Matthias Rief   +2 more
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Expression and Purification of Maltose‐Binding Protein Fusions

Current Protocols in Molecular Biology, 1994
AbstractThis 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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Protein Purification with C-Terminal Fusion of Maltose Binding Protein

Protein Expression and Purification, 1998
For 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 ...
Lars Hennig, Eberhard Schäfer
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