title: The smallest active fragment of microtubule-associated protein 4 and its interaction with microtubules in phosphate buffer.
abstract: To analyze the interaction between microtubule-associated protein (MAP) 4 and microtubules physicochemically, a MAP4 active site fragment was designed for nuclear magnetic resonance (NMR) use. The fragment was bacterially expressed and purified to homogeneity. The buffer conditions for NMR were optimized to support microtubule assembly. The fragment was found to bind to microtubules under the optimized buffer conditions.
authors.affiliation: Department of Biological Sciences, Faculty of Science, Kanagawa University, Hiratsuka, Kanagawa, Japan. r201070258yd@kanagawa-u.ac.jp
authors.forename: Yurika
authors.initials: Y
authors.lastname: Hashi
authors.forename: Lisa
authors.initials: L
authors.lastname: Nagase
authors.forename: Kazuyuki
authors.initials: K
authors.lastname: Matsushima
authors.forename: Susumu
authors.initials: S
authors.lastname: Kotani
mesh_terms: D002021:Buffers; D009682:Magnetic Resonance Spectroscopy; D008869:Microtubule-Associated Proteins / Q000737:chemistry* / Q000378:metabolism; D008870:Microtubules / Q000378:metabolism*; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism*; D010710:Phosphates / Q000737:chemistry*; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D002021:Buffers; D008869:Microtubule-Associated Proteins; D010446:Peptide Fragments; D010710:Phosphates