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Cryo-EM Structure of the Flagellar Motor Complex from <i>Paenibacillus</i> sp. TCA20. [PDF]
Onoe S+8 more
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Branched oligosaccharides cause atypical starch granule initiation in Arabidopsis chloroplasts. [PDF]
Heutinck AJM+7 more
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SMCT1 has a low affinity to PDZ domain containing 1 protein. [PDF]
Zhang Q, Clinton J, Westerlund K, Mim C.
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Structure of a transcribing Pol II-DSIF-SPT6-U1 snRNP complex
Zhang L+7 more
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Purification of proteins fused to maltose-binding protein. [PDF]
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
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Programming Xenon Diffusion in Maltose Binding Protein
SSRN Electronic Journal, 2022Protein 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 ...
Zhuangyu Zhao+3 more
openaire +2 more sources
Expression and purification of recombinant proteins by fusion to maltose-binding protein
Molecular Biotechnology, 2000The pMAL vectors provide a method for purifying proteins from cloned genes by fusing them to maltose-binding protein (MBP, product of malE), which binds to amylose. The vectors use the tac promoter and the translation initiation signals of MBP to give high-level expression of the fusion, and an affinity purification for MBP to isolate the fusion ...
P. Riggs
semanticscholar +3 more sources
Maltodextrin-modified magnetic microspheres for selective enrichment of maltose binding proteins.
ACS Applied Materials and Interfaces, 2014In this work, maltodextrin-modified magnetic microspheres Fe3O4@SiO2-Maltodextrin (Fe3O4@SiO2-MD) with uniform size and fine morphology were synthesized through a facile and low-cost method.
Jin Zheng+6 more
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Ligand-induced structural changes in maltose binding proteins measured by atomic force microscopy.
Nano letters (Print), 2008We use atomic force microscopy (AFM) based force-compression measurements to probe the ligand-induced functional conformational changes in surface-immobilized dicysteine-terminated maltose binding proteins (dicys-MBPs).
C. Staii, D. Wood, G. Scoles
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