Ligand-modulated parallel mechanical unfolding pathways of maltose-binding proteins. [PDF]
J Biol Chem, 2011 Protein folding and unfolding are complex phenomena, and it is accepted that multidomain proteins generally follow multiple pathways. Maltose-binding protein (MBP) is a large (a two-domain, 370-amino acid residue) bacterial periplasmic protein involved ...
Aggarwal V +5 more
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Competitive interactions of ligands and macromolecular crowders with maltose binding protein. [PDF]
PLoS ONE, 2013 Cellular signaling involves a cascade of recognition events occurring in a complex environment with high concentrations of proteins, polysaccharides, and other macromolecules.
Andrew C Miklos +2 more
doaj +6 more sources
Structure of an engineered β-lactamase maltose binding protein fusion protein: insights into heterotropic allosteric regulation. [PDF]
PLoS ONE, 2012 Engineering novel allostery into existing proteins is a challenging endeavor to obtain novel sensors, therapeutic proteins, or modulate metabolic and cellular processes.
Wei Ke +8 more
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Exploring the Unfolding Pathway of Maltose Binding Proteins: An Integrated Computational Approach [PDF]
Journal of Chemical Theory and Computation, 2014 Recent single-molecule force spectroscopy experiments on the Maltose Binding Proteins (MBPs) identified four stable structural units, termed unfoldons, that resist mechanical stress and determine the intermediates of the unfolding pathway.
Carlo Guardiani +4 more
semanticscholar +9 more sources
Accessing a hidden conformation of the maltose binding protein using accelerated molecular dynamics.
PLoS Computational Biology, 2011 Periplasmic binding proteins (PBPs) are a large family of molecular transporters that play a key role in nutrient uptake and chemotaxis in Gram-negative bacteria.
Denis Bucher +3 more
doaj +3 more sources
Differential Substrate Recognition by Maltose Binding Proteins Influenced by Structure and Dynamics. [PDF]
Biochemistry, 2018 The genome of the hyperthermophile Thermotoga maritima contains three isoforms of maltose binding protein (MBP) that are high-affinity receptors for di-, tri-, and tetrasaccharides.
Shukla S +5 more
europepmc +2 more sources
Structure dictates the mechanism of ligand recognition in the histidine and maltose binding proteins [PDF]
Current Research in Structural Biology, 2020 Two mechanisms, induced fit (IF) and conformational selection (CS), have been proposed to explain ligand recognition coupled conformational changes. The histidine binding protein (HisJ) adopts the CS mechanism, in which a pre-equilibrium is established ...
Lakshmi P. Jayanthi +2 more
doaj +2 more sources
Maltose-Binding Protein (MBP), a Secretion-Enhancing Tag for Mammalian Protein Expression Systems. [PDF]
PLoS ONE, 2016 Recombinant proteins are commonly expressed in eukaryotic expression systems to ensure the formation of disulfide bridges and proper glycosylation. Although many proteins can be expressed easily, some proteins, sub-domains, and mutant protein versions ...
Raphael Reuten +7 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]
PLoS 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 large, general and modular DARPin–apoferritin scaffold enables the visualization of small proteins by cryo-EM [PDF]
IUCrJSingle-particle cryo-electron microscopy (cryo-EM) has emerged as an indispensable technique in structural biology that is pivotal for deciphering protein architectures. However, the medium-sized proteins (30–40 kDa) that are prevalent in both eukaryotic
Xin Lu +11 more
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