Pharmaceutics, 2022 Protein modification with non-canonical amino acids (ncAAs) represents a useful technology to afford homogenous samples of bioconjugates with site-specific modification.
Alexander C. Williard +10 more
doaj +1 more source
Folding of maltose-binding protein. Evidence for the identity of the rate-determining step in vivo and in vitro. [PDF]
, 1993 The folding of maltose-binding protein, a periplasmic protein in Escherichia coli, was shown to proceed through the same rate-limiting step whether folding occurred in the cell under physiological conditions or in vitro in the absence of other proteins ...
So‐Young Chun +3 more
openalex +3 more sources
Thermodynamics of maltose binding protein unfolding [PDF]
Protein Science, 1997 AbstractThe maltose binding protein (MBP or MalE) of Escherichia coli is the periplasmic component of the transport system for malto‐oligosaccharides. It is used widely as a carrier protein for the production of recombinant fusion proteins. The melting of recombinant MBP was studied by differential scanning and titration calorimetry and fluorescence ...
Kenneth C. Ingham, Valery Novokhatny
openaire +3 more sources
Backbone assignment of crystalline E. coli maltose binding protein [PDF]
Biomolecular NMR Assignments, 2021 The E.coli maltose binding protein (MBP) is a 42.5 kDa molecule widely employed in many biotechnology applications. Because of its molecular size, it has become the main model system for the development of solution NMR methods adapted to large biomolecular targets.
Tobias Schubeis +2 more
openaire +5 more sources
Spectroscopic properties of an engineered maltose binding protein [PDF]
Protein Engineering Design and Selection, 1997 The maltose binding protein (MBP) has been site specifically labelled with a nitrobenzoxadiazole (NBD) group following mutation of a serine to a cysteine residue at position 337. The resulting protein shows a large ligand (maltose or beta-cyclodextrin) dependent increase in its steady-state fluorescence intensity.
GILARDI, Gianfranco +4 more
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Maltoporins and maltose-binding proteins of Yersinia enterocolitica [PDF]
Journal of General Microbiology, 1993 Two components of the Yersinia enterocolitica maltose transport system, maltoporin (OmpM) and an osmotically shockable periplasmic maltose-binding protein (MBP) were identified. The synthesis of OmpM (apparent Mr 43,000) and transport of maltose into cells of Y. enterocolitica were induced by maltose and maltodextrins.
Jerzy Hrebenda +2 more
openaire +3 more sources
Crystallization, data collection and data processing of maltose-binding protein (MalE) from the phytopathogen Xanthomonas axonopodis pv. citri [PDF]
, 2009 Maltose-binding protein is the periplasmic component of the ABC transporter responsible for the uptake of maltose/maltodextrins. The Xanthomonas axonopodis pv.
Balan, A. +4 more
core +2 more sources
Maltose and maltodextrin utilization by Listeria monocytogenes depend on an inducible ABC transporter which is repressed by glucose. [PDF]
PLoS ONE, 2010 In the environment as well as in the vertebrate intestine, Listeriae have access to complex carbohydrates like maltodextrins. Bacterial exploitation of such compounds requires specific uptake and utilization systems.We could show that Listeria ...
Shubha Gopal +6 more
doaj +1 more source
Dependence of protein-induced lipid bilayer deformations on protein shape [PDF]
, 2022 Membrane proteins typically deform the surrounding lipid bilayer membrane, which can play an important role in the function, regulation, and organization of membrane proteins. Membrane elasticity theory provides a beautiful description of protein-induced lipid bilayer deformations, in which all physical parameters can be directly determined from ...
arxiv +1 more source
Selectivity for maltose and maltodextrins of maltoporin, a pore-forming protein of E. coli outer membrane [PDF]
, 1987 Homogeneous maltoporin (lamB protein), an Escherichia coli outer membrane spanning protein, was incorporated in phospholipid planar bilayers. It generates aqueous channels distinct from those formed by the non-specific porin (OmpF) or by phosphoporin ...
Dargent, Bénédicte +2 more
core +1 more source