10 research outputs found
Preparation of dual-function chelating resin with high capacity and adjustable adsorption selectivity to variety of heavy metal ions
Multidentate boronate magnetic adsorbent assembled with polyhedral oligomeric silsesquioxanes and intramolecular diboronic acid for improving the binding strength toward glycoproteins
Zirconium-doped magnetic microspheres for the selective enrichment of cis-diol-containing ribonucleosides
Preparation of a boronate affinity material with ultrahigh binding capacity for cis-diols by grafting polymer brush from polydopamine-coated magnetized graphene oxide
A magnetic adsorbent grafted with pendant naphthyl polymer brush for enrichment of the nonsteroidal anti-inflammatory drugs indomethacin and diclofenac
Preparation of bottlebrush polymer–modified magnetic graphene as immobilized metal ion affinity adsorbent for purification of hemoglobin from blood samples
Tunable composites prepared from graphene oxide and zeolitic imidazolate framework-8 for improved selective isolation of hemoglobin
Structural analysis of the complex between calmodulin and full-length myelin basic protein, an intrinsically disordered molecule.
Myelin basic protein (MBP) is present between the cytoplasmic leaflets of the compact myelin membrane in both the peripheral and central nervous systems, and characterized to be intrinsically disordered in solution. One of the best-characterized protein ligands for MBP is calmodulin (CaM), a highly acidic calcium sensor. We pulled down MBP from human brain white matter as the major calcium-dependent CaM-binding protein. We then used full-length brain MBP, and a peptide from rodent MBP, to structurally characterize the MBP-CaM complex in solution by small-angle X-ray scattering, NMR spectroscopy, synchrotron radiation circular dichroism spectroscopy, and size exclusion chromatography. We determined 3D structures for the full-length protein-protein complex at different stoichiometries and detect ligand-induced folding of MBP. We also obtained thermodynamic data for the two CaM-binding sites of MBP, indicating that CaM does not collapse upon binding to MBP, and show that CaM and MBP colocalize in myelin sheaths. In addition, we analyzed the post-translational modifications of rat brain MBP, identifying a novel MBP modification, glucosylation. Our results provide a detailed picture of the MBP-CaM interaction, including a 3D model of the complex between full-length proteins