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MBP, Maltose binding protein

Abbreviations c-Abl, Abelson protein tyrosine kinase c-Crk-II, CTIO regulator of kinase Csk, C-terminal Src kinase GFP, green fluorescent protein Hpal, restriction endonuclease from Haemophilus parainfluenzae MBP, maltose-binding protein SHP-2, Src homology 2 protein tyrosine phosphatase Src, Rous sarcoma vims kinase. [Pg.107]

Figure 29 Schematic representation of the QD-dye-labeled protein conjugate (DHLA dihydroUpoic acid, a water-soluble capping ligand MBP maltose binding protein Dye AlexaFluor 488 or Cy3) used to investigate the properties of QDs as acceptors in FRET processes. (Reproduced with permission from Ref. 64. 2005, American Chemical Society.)... Figure 29 Schematic representation of the QD-dye-labeled protein conjugate (DHLA dihydroUpoic acid, a water-soluble capping ligand MBP maltose binding protein Dye AlexaFluor 488 or Cy3) used to investigate the properties of QDs as acceptors in FRET processes. (Reproduced with permission from Ref. 64. 2005, American Chemical Society.)...
Proteins expressed as fusion proteins have also been crystallized. Maltose binding protein (MBP) (Kobe et al., 1999 Liu et al., 2001), thioredoxin (Stoll et al., 1998) and GST (Kuge et al., 1997) have all been used as fusion proteins in structure studies. [Pg.471]

The His-tagged MBP-MS2 coat fusion protein (HMM) used in this method was created to allow the protein to be immobilized on both Ni2+ or amylose affinity resins. HMM is a 59-kDa protein containing an NT-terminal hexahistidine (6x His) tag, a central maltose-binding protein (MBP) domain, and a C-terminal MS2 coat protein containing the V29/dIFG mutations, which prevent protein multimerization and increase its affinity for RNA (Lim and Peabody, 1994). The protein is expressed in E. coli from plasmid pHMM, which confers kanamycin resistance, and purified using affinity chromatography. [Pg.9]

MBP Myelin basic protein maltose-binding protein... [Pg.14]

Fig. 1. H- - C CT-HSQC spectrum of a sample of 1.5mM Val, Leu, lie (51) methyl-protonated maltose-binding protein (MBP), 2mM /3-cyclodextrin, 20 mM sodium phosphate (pH 7.2), 3mM NaN(, 200pM EDTA, 0. 1 mg/ml Pefabloc, 1 /ig//d pepstatin and 10% D20 recorded at 37°C, on a Varian Unity-1- 500-MHz spectrometer. Acquisition times of 28 and 64 ms were employed (/, t2) along with a relaxation delay of 1.5 s, fora total measuring time of 3 h. (a) Aliphatic region of the H- - C correlation map of MBP, illustrating the selectivity of labelling. Small amounts of residual protonation are observed at the Cy positions of a number of Pro/Arg residues, the Cp positions of Asp and Ser (aliased) residues, and the Cy2 methyl positions of lie. In all cases, intensities of these cross-peaks are less than 10% of the methyl peaks, (b) Methyl region of the H- - C HSQC. Reproduced with permission from Kluwer Academic Publishers Goto et al.H... Fig. 1. H- - C CT-HSQC spectrum of a sample of 1.5mM Val, Leu, lie (51) methyl-protonated maltose-binding protein (MBP), 2mM /3-cyclodextrin, 20 mM sodium phosphate (pH 7.2), 3mM NaN(, 200pM EDTA, 0. 1 mg/ml Pefabloc, 1 /ig//d pepstatin and 10% D20 recorded at 37°C, on a Varian Unity-1- 500-MHz spectrometer. Acquisition times of 28 and 64 ms were employed (/, t2) along with a relaxation delay of 1.5 s, fora total measuring time of 3 h. (a) Aliphatic region of the H- - C correlation map of MBP, illustrating the selectivity of labelling. Small amounts of residual protonation are observed at the Cy positions of a number of Pro/Arg residues, the Cp positions of Asp and Ser (aliased) residues, and the Cy2 methyl positions of lie. In all cases, intensities of these cross-peaks are less than 10% of the methyl peaks, (b) Methyl region of the H- - C HSQC. Reproduced with permission from Kluwer Academic Publishers Goto et al.H...
As a variant of the studies discussed above, Lecroisey et al.1] undertook an NMR study of the 11 amino acid C3 epitope from poliovirus VP1 following its insertion at eight different sites into maltose-binding protein (MBP) (mass 41 kDa). The insertion of this epitope at the various sites did not cause significant structural changes to the protein so as to affect its ability to function normally and bind maltose. From H NMR studies of these mutants, it was found that the epitope had significant conformational flexibility and that the mobility was maintained regardless of where it was placed into the protein.71 Consistent with this mobility, the epitope adopted no ordered conformation in any of the mutants. [Pg.42]

MBP (biotinylated) Biotinylated E. coli maltose-binding protein Panning in solution followed by capture on streptavidin-magnetic beads... [Pg.243]

A rather widespread family of proteins, found in the periplasmic space of gramnegative bacteria, complexes certain small molecules and allows them to be transported through the cell wall or activate chemotaxis. Each of these functions involves a consecutive interaction with specific membrane proteins. The molecules transported are amino acids, sulfate, mono- and oligosaccchrides. In this way ABP complexes L-arabinose (K 0.98 x 10 M), and MBP (maltodextrin-binding protein) complexes maltose (ATj 35 x 10 M) and maltodextrins. It is in this series that are found the strongest possible bonds between sugars and proteins. The dissociation rate ( i 1.5 s ) is indicative of the upper limit of the ionic transport rate. Hydrogen bonds... [Pg.125]


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See also in sourсe #XX -- [ Pg.558 ]




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Maltose binding protein

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