Results 261 to 270 of about 73,040 (302)

Purification of Proteins Fused to Maltose-Binding Protein

2010
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.
Mario, Lebendiker, Tsafi, Danieli
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Tritium NMR spectroscopy of ligand binding to maltose-binding protein

Biochemistry, 1991
Tritium-labeled alpha- and beta-maltodextrins have been used to study their complexes with maltose-binding protein (MBP), a 40-kDa bacterial protein. Five substrates, from maltose to maltohexaose, were labeled at their reducing ends and their binding studied.
K, Gehring, P G, Williams, J G, Pelton, H, Morimoto, D E, Wemmer   +4 more
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How maltose influences structural changes to bind to maltose‐binding protein: Results from umbrella sampling simulation

Proteins: Structure, Function, and Bioinformatics, 2012
AbstractA well‐studied periplasmic‐binding protein involved in the abstraction of maltose is maltose‐binding protein (MBP), which undergoes a ligand‐induced conformational transition from an open (ligand‐free) to a closed (ligand‐bound) state. Umbrella sampling simulations have been us to estimate the free energy of binding of maltose to MBP and to ...
Nahren Manuel, Mascarenhas, Johannes, Kästner   +1 more
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Maltose and Maltotriose Derivatives as Potential Inhibitors of the Maltose‐Binding Protein

European Journal of Organic Chemistry, 2008
AbstractInhibition of substrate binding to maltose‐binding protein (MBP) was investigated with structurally modified maltose and maltotriose derivatives that were designed based on the X‐ray analysis of maltose and maltotriose bound to MBP. In maltose, positions 1a, 2a, 2b, 4b and 6b were modified (compounds 1–3, 18a, b, 28a–c, 39 and 44) of which only
Heinz Malik, Winfried Boos, Richard R. Schmidt   +2 more
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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 ...
L, Hennig, E, Schäfer
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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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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
Igor L, Medintz, Jeffrey R, Deschamps
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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 ...
G, Gilardi, L Q, Zhou, L, Hibbert, A E, Cass   +3 more
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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
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Associative properties of the Escherichiacoli galactose binding protein and maltose binding protein

Biochemical and Biophysical Research Communications, 1982
The ligand-binding characteristics of periplasmic galactose-binding protein and maltose-binding protein of Escherichia coli are analyzed. The saturation function was decreased upon increasing protein concentration and the monomer-dimer equilibrium was shifted towards the monomeric protein form upon an increase of the ligand concentration.
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