The Binding of Maltose to 'Virgin' Maltose-Binding Protein is Biphasic
نویسندگان
چکیده
منابع مشابه
Engineered Derivatives of Maltose-Binding Protein
Maltose-binding protein (MBP), a member of the periplasmic binding protein family of Gram negative bacteria, is a versatile substrate for protein engineering. In common with other periplasmic proteins, it is extremely protease resistant, and it can fold properly in both the cytoplasmic and periplasmic compartments. It binds a variety of glucose-14-glucose polysaccharides, from maltose and lon...
متن کاملMaltose-binding protein as a solubility enhancer.
1. Introduction A major impediment to the production of recombinant proteins in Escheri-chia coli is their tendency to accumulate in the form of insoluble and biologically inactive aggregates known as inclusion bodies. Although it is sometimes possible to convert aggregated material into native, biologically-active protein , this is a time consuming, labor-intensive, costly, and uncertain under...
متن کاملDependence of maltose transport and chemotaxis on the amount of maltose-binding protein.
Maltose-binding protein (MBP) is essential for maltose transport and chemotaxis in Escherichia coli. To perform these functions it must interact with two sets of cytoplasmic membrane proteins, the MalFGK transport complex and the chemotactic signal transducer Tar. MBP is present at high concentrations, on the order of 1 mM, in the periplasm of maltose-induced or malTc constitutive cells. To det...
متن کاملMaltose-binding protein is a potential carrier for oral immunizations.
Maltose binding protein (MBP) is often fused to a relevant protein to improve its yield and facilitate its purification, but MBP can also enhance the immunogenicity of the fused proteins. Recent data suggest that MBP may potentiate antigen-presenting functions in immunized animals by providing intrinsic maturation stimuli to dendritic cells through TLR4. The aim of this study was to examine if ...
متن کاملThe energetics of structural change in maltose-binding protein.
H igh-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. However, as many experiments have shown, some specific interactions that look...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1975
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1975.tb21022.x