Results 11 to 20 of about 940,374 (326)

Engineered Derivatives of Maltose-Binding Protein [PDF]

open access: hybrid, 2012
Maltose-binding protein (MBP), a member of the periplasmic binding protein family of Gram negative bacteria, is a versatile substrate for protein engineering.
Dipak Paul
semanticscholar   +6 more sources

Discovery of an auto-regulation mechanism for the maltose ABC transporter MalFGK2. [PDF]

open access: yesPLoS ONE, 2012
The maltose transporter MalFGK(2), together with the substrate-binding protein MalE, is one of the best-characterized ABC transporters. In the conventional model, MalE captures maltose in the periplasm and delivers the sugar to the transporter.
Huan Bao, Franck Duong
doaj   +21 more sources

Programming xenon diffusion in maltose-binding protein. [PDF]

open access: yesBiophys J, 2022
Protein 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 ...
Zhao Z, Rudman NA, He J, Dmochowski IJ.
europepmc   +3 more sources

Open and Closed Form of Maltose Binding Protein in Its Native and Molten Globule State As Studied by Electron Paramagnetic Resonance Spectroscopy. [PDF]

open access: yesBiochemistry, 2018
An intensively investigated intermediate state of protein folding is the molten globule (MG) state, which contains secondary but hardly any tertiary structure.
Selmke B   +5 more
europepmc   +2 more sources

Purity of maltose-binding protein – Recombinant streptavidin expressed in Escherichia coli BL21 (pD861-MBP: 327892) [PDF]

open access: yesJournal of Advanced Pharmaceutical Technology & Research, 2022
Nearly 95% of streptavidin which is expressed in Escherichia coli found as an inclusion body. Protein expressed in an inclusion body form requires further steps for the folding process related to its purification.
Toto Subroto   +5 more
doaj   +2 more sources

Heterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusions. [PDF]

open access: yesPLoS ONE, 2013
The expression of heteroligomeric protein complexes for structural studies often requires a special coexpression strategy. The reason is that the solubility and proper folding of each subunit of the complex requires physical association with other ...
Mark A Arbing   +14 more
doaj   +2 more sources

A useful epitope tag derived from maltose binding protein. [PDF]

open access: yesProtein Sci, 2021
AbstractMaltose binding protein (MBP) is used in recombinant protein expression as an affinity and solubility tag. The monoclonal antibody B48 binds MBP tightly and has no cross‐reactivity to other proteins in an Escherichia coli lysate. This high level of specificity suggested that MBP contains an epitope that could prove useful as a purification and ...
Lénon M   +6 more
europepmc   +4 more sources

The energetics of structural change in maltose-binding protein [PDF]

open access: greenProceedings of the National Academy of Sciences, 2003
High-resolution structures of proteins and their complexes are now appearing in the Research Collaboratory for Structural Bioinformatics (RCSB) database at a tremendous rate. When analyzing the structures of proteins, it is often tempting to try to extract energetic contributions to stability or binding interactions.
David E. Wemmer
openalex   +4 more sources

Exploration of multi-state conformational dynamics and underlying global functional landscape of maltose binding protein. [PDF]

open access: yesPLoS Computational Biology, 2012
An increasing number of biological machines have been revealed to have more than two macroscopic states. Quantifying the underlying multiple-basin functional landscape is essential for understanding their functions. However, the present models seem to be
Yong Wang   +3 more
doaj   +2 more sources

Molecular analysis of cyclic α-maltosyl-(1→6)-maltose binding protein in the bacterial metabolic pathway. [PDF]

open access: yesPLoS ONE, 2020
Cyclic α-maltosyl-(1→6)-maltose (CMM) is a cyclic glucotetrasaccharide with alternating α-1,4 and α-1,6 linkages. Here, we report functional and structural analyses on CMM-binding protein (CMMBP), which is a substrate-binding protein (SBP) of an ABC ...
Masaki Kohno   +6 more
doaj   +2 more sources

Home - About - Disclaimer - Privacy