Results 71 to 80 of about 940,374 (326)

The Major Soybean Allergen Gly m Bd 28K Induces Hypersensitivity Reactions in Mice Sensitized to Cow's Milk Proteins [PDF]

open access: yes, 2016
Reactions to soy have been reported in a proportion of patients with IgE-mediated cow’s milk allergy (CMA). In this work, we analyzed if Gly m Bd 28K/P28, one of the major soybean allergens, is a cross-reactive allergen with cow milk proteins (CMP).
Candreva, Ángela María   +5 more
core   +2 more sources

Role of Water in Ligand Binding to Maltose-Binding Protein: Insight from a New Docking Protocol Based on the 3D-RISM-KH Molecular Theory of Solvation

open access: yesJournal of Chemical Information and Modeling, 2015
Maltose-binding protein is a periplasmic binding protein responsible for transport of maltooligosaccarides through the periplasmic space of Gram-negative bacteria, as a part of the ABC transport system.
Wenjuan Huang   +3 more
semanticscholar   +1 more source

Location of tolerated insertions/deletions in the structure of the maltose binding protein [PDF]

open access: yesFEBS Letters, 1993
In a previous study [(1987) J. Mol. Biol. 194, 663‐673], we isolated ten insertion/deletion mutants (indels) of the maltose binding protein for which the maltose binding constant was only a little or not at all affected. In this paper, we have localized these mutations in the recently solved three‐dimensional structure.
Maurice Hofnung   +3 more
openaire   +3 more sources

Mutations in maltose-binding protein that alter affinity and solubility properties [PDF]

open access: yesApplied Microbiology and Biotechnology, 2010
Maltose-binding protein (MBP) from Escherichia coli has been shown to be a good substrate for protein engineering leading to altered binding (Marvin and Hellinga, Proc Natl Acad Sci U S A 98:4955-4960, 2001a) and increased affinity (Marvin and Hellinga, Nat Struct Biol 8:795-798, 2001b; Telmer and Shilton, J Biol Chem 278:34555-34567, 2003). It is also
Pei-Chung Hsieh   +2 more
openaire   +3 more sources

Recombinant expression and purification of an Oxysterol Binding Protein from Aspergillus oryzae 3.042

open access: yesBIO Web of Conferences, 2017
A full-length cDNA encoding a candidate Oxysterol-binding protein(OSBP) from Aspergillus oryzae (AoOSBP) was cloned and expressed in Escherichia coli as a maltose-binding protein (MBP) fusion protein.
Zhang Xian   +4 more
doaj   +1 more source

Expression and Purification of the Arabidopsis E4 SUMO Ligases PIAL1 and PIAL2

open access: yesBio-Protocol, 2015
The proteins PIAL1 (At1g08910) and PIAL2 (At5g41580) are members of the recently discovered group of plant E4 SUMO ligases. This protocol allows quick and simple expression of the recombinant proteins in Escherichia coli (E.
Konstantin Tomanov, Andreas Bachmair
doaj   +1 more source

Virtual Identification of Essential Proteins Within the Protein Interaction Network of Yeast [PDF]

open access: yes, 2005
Topological analysis of large scale protein-protein interaction networks (PINs) is important for understanding the organisational and functional principles of individual proteins. The number of interactions that a protein has in a PIN has been observed to be correlated with its indispensability.
arxiv   +1 more source

The Binding of Maltose to ‘Virgin’ Maltose‐Binding Protein is Biphasic [PDF]

open access: yesEuropean Journal of Biochemistry, 1975
The biphasic binding properties of the galactose‐binding and maltose‐binding proteins of Escherichia coli may be important in the functioning of these proteins as recognition components of chemoreceptors. However, Richarme and Kepes [Eur. J. Biochem. 45, 127‐133 (1974)] have suggested that the biphasic binding curve of the galactose‐binding protein may
openaire   +3 more sources

Stimulation of the Maltose Transporter ATPase by Unliganded Maltose Binding Protein [PDF]

open access: yesBiochemistry, 2009
ATP hydrolysis by the maltose transporter (MalFGK(2)) is regulated by maltose binding protein (MBP). Binding of maltose to MBP brings about a conformational change from open to closed that leads to a strong stimulation of the MalFGK(2) ATPase. In this study, we address the long-standing but enigmatic observation that unliganded MBP is also able to ...
Gould, Alister D.   +2 more
openaire   +5 more sources

Purifying natively folded proteins from inclusion bodies using sarkosyl, Triton X-100, and CHAPS

open access: yesBioTechniques, 2010
We describe a rapid, simple, and efficient method for recovering glutathione S-transferase (GST)- and His6-tagged maltose binding protein (MBP) fusion proteins from inclusion bodies.
Hu Tao   +5 more
doaj   +1 more source

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