Review



bacterial maltose binding protein  (Novus Biologicals)


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    Structured Review

    Novus Biologicals bacterial maltose binding protein
    ( a ) Quantification of a monolinked peptide from <t>maltose</t> <t>binding</t> <t>protein</t> (MBP) with or without maltose. Structures of MBP in the open, ligand-free conformation (green, 1mpb.pdb) and the closed, maltose-bound conformation (brown, 1n3w.pdb) are shown on the left. A close-up view of the ‘balancing interface’ is shown on the right. In the closed conformation, the sequence between amino acids 301–312 forms an alpha helix (gray) and K313 forms a salt bridge with E310. The helix and the salt bridge are disrupted in the open conformation (cyan). A crosslinker swapping experiment was performed on the same preparation of MBP; a technical replicate. ( b ) Quantification of monolinked and crosslinked peptides involving K78 and K95 from apo-CaM and CaM with Ca 2+ and CBP. Structures of apo-CaM (left) and CaM + CBP (blue) + Ca 2+ (right) are shown with key lysine residues space filled and magenta. The experiment was performed once.
    Bacterial Maltose Binding Protein, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 92/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/bacterial+maltose+binding+protein/pmc11563578-266-0-7?v=Novus+Biologicals
    Average 92 stars, based on 3 article reviews
    bacterial maltose binding protein - by Bioz Stars, 2026-07
    92/100 stars

    Images

    1) Product Images from "Isobaric crosslinking mass spectrometry technology for studying conformational and structural changes in proteins and complexes"

    Article Title: Isobaric crosslinking mass spectrometry technology for studying conformational and structural changes in proteins and complexes

    Journal: eLife

    doi: 10.7554/eLife.99809

    ( a ) Quantification of a monolinked peptide from maltose binding protein (MBP) with or without maltose. Structures of MBP in the open, ligand-free conformation (green, 1mpb.pdb) and the closed, maltose-bound conformation (brown, 1n3w.pdb) are shown on the left. A close-up view of the ‘balancing interface’ is shown on the right. In the closed conformation, the sequence between amino acids 301–312 forms an alpha helix (gray) and K313 forms a salt bridge with E310. The helix and the salt bridge are disrupted in the open conformation (cyan). A crosslinker swapping experiment was performed on the same preparation of MBP; a technical replicate. ( b ) Quantification of monolinked and crosslinked peptides involving K78 and K95 from apo-CaM and CaM with Ca 2+ and CBP. Structures of apo-CaM (left) and CaM + CBP (blue) + Ca 2+ (right) are shown with key lysine residues space filled and magenta. The experiment was performed once.
    Figure Legend Snippet: ( a ) Quantification of a monolinked peptide from maltose binding protein (MBP) with or without maltose. Structures of MBP in the open, ligand-free conformation (green, 1mpb.pdb) and the closed, maltose-bound conformation (brown, 1n3w.pdb) are shown on the left. A close-up view of the ‘balancing interface’ is shown on the right. In the closed conformation, the sequence between amino acids 301–312 forms an alpha helix (gray) and K313 forms a salt bridge with E310. The helix and the salt bridge are disrupted in the open conformation (cyan). A crosslinker swapping experiment was performed on the same preparation of MBP; a technical replicate. ( b ) Quantification of monolinked and crosslinked peptides involving K78 and K95 from apo-CaM and CaM with Ca 2+ and CBP. Structures of apo-CaM (left) and CaM + CBP (blue) + Ca 2+ (right) are shown with key lysine residues space filled and magenta. The experiment was performed once.

    Techniques Used: Binding Assay, Sequencing


    Figure Legend Snippet:

    Techniques Used: Recombinant, Binding Assay, Software



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    ( a ) Quantification of a monolinked peptide from <t>maltose</t> <t>binding</t> <t>protein</t> (MBP) with or without maltose. Structures of MBP in the open, ligand-free conformation (green, 1mpb.pdb) and the closed, maltose-bound conformation (brown, 1n3w.pdb) are shown on the left. A close-up view of the ‘balancing interface’ is shown on the right. In the closed conformation, the sequence between amino acids 301–312 forms an alpha helix (gray) and K313 forms a salt bridge with E310. The helix and the salt bridge are disrupted in the open conformation (cyan). A crosslinker swapping experiment was performed on the same preparation of MBP; a technical replicate. ( b ) Quantification of monolinked and crosslinked peptides involving K78 and K95 from apo-CaM and CaM with Ca 2+ and CBP. Structures of apo-CaM (left) and CaM + CBP (blue) + Ca 2+ (right) are shown with key lysine residues space filled and magenta. The experiment was performed once.
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    ( a ) Quantification of a monolinked peptide from <t>maltose</t> <t>binding</t> <t>protein</t> (MBP) with or without maltose. Structures of MBP in the open, ligand-free conformation (green, 1mpb.pdb) and the closed, maltose-bound conformation (brown, 1n3w.pdb) are shown on the left. A close-up view of the ‘balancing interface’ is shown on the right. In the closed conformation, the sequence between amino acids 301–312 forms an alpha helix (gray) and K313 forms a salt bridge with E310. The helix and the salt bridge are disrupted in the open conformation (cyan). A crosslinker swapping experiment was performed on the same preparation of MBP; a technical replicate. ( b ) Quantification of monolinked and crosslinked peptides involving K78 and K95 from apo-CaM and CaM with Ca 2+ and CBP. Structures of apo-CaM (left) and CaM + CBP (blue) + Ca 2+ (right) are shown with key lysine residues space filled and magenta. The experiment was performed once.
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    Novus Biologicals recombinant protein bacterial maltose binding protein

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    Image Search Results


    ( a ) Quantification of a monolinked peptide from maltose binding protein (MBP) with or without maltose. Structures of MBP in the open, ligand-free conformation (green, 1mpb.pdb) and the closed, maltose-bound conformation (brown, 1n3w.pdb) are shown on the left. A close-up view of the ‘balancing interface’ is shown on the right. In the closed conformation, the sequence between amino acids 301–312 forms an alpha helix (gray) and K313 forms a salt bridge with E310. The helix and the salt bridge are disrupted in the open conformation (cyan). A crosslinker swapping experiment was performed on the same preparation of MBP; a technical replicate. ( b ) Quantification of monolinked and crosslinked peptides involving K78 and K95 from apo-CaM and CaM with Ca 2+ and CBP. Structures of apo-CaM (left) and CaM + CBP (blue) + Ca 2+ (right) are shown with key lysine residues space filled and magenta. The experiment was performed once.

    Journal: eLife

    Article Title: Isobaric crosslinking mass spectrometry technology for studying conformational and structural changes in proteins and complexes

    doi: 10.7554/eLife.99809

    Figure Lengend Snippet: ( a ) Quantification of a monolinked peptide from maltose binding protein (MBP) with or without maltose. Structures of MBP in the open, ligand-free conformation (green, 1mpb.pdb) and the closed, maltose-bound conformation (brown, 1n3w.pdb) are shown on the left. A close-up view of the ‘balancing interface’ is shown on the right. In the closed conformation, the sequence between amino acids 301–312 forms an alpha helix (gray) and K313 forms a salt bridge with E310. The helix and the salt bridge are disrupted in the open conformation (cyan). A crosslinker swapping experiment was performed on the same preparation of MBP; a technical replicate. ( b ) Quantification of monolinked and crosslinked peptides involving K78 and K95 from apo-CaM and CaM with Ca 2+ and CBP. Structures of apo-CaM (left) and CaM + CBP (blue) + Ca 2+ (right) are shown with key lysine residues space filled and magenta. The experiment was performed once.

    Article Snippet: Bacterial maltose binding protein was purchased from Novus Biologicals (Littleton, CO).

    Techniques: Binding Assay, Sequencing

    Journal: eLife

    Article Title: Isobaric crosslinking mass spectrometry technology for studying conformational and structural changes in proteins and complexes

    doi: 10.7554/eLife.99809

    Figure Lengend Snippet:

    Article Snippet: Bacterial maltose binding protein was purchased from Novus Biologicals (Littleton, CO).

    Techniques: Recombinant, Binding Assay, Software

    Journal: eLife

    Article Title: Isobaric crosslinking mass spectrometry technology for studying conformational and structural changes in proteins and complexes

    doi: 10.7554/eLife.99809

    Figure Lengend Snippet:

    Article Snippet: Peptide, recombinant protein , Bacterial maltose binding protein , Novus Biologicals , Cat# NBC118538 , .

    Techniques: Recombinant, Binding Assay, Software