Laboratory of Protein Folding


Director Yuji GOTO
Associate Prof. (Lecturer) Kenji SASAHARA
Assistant Prof. Masatomo SO
Specially Appointed Assistant Prof. Keiichi YAMAGUCHI



Tel 81-6-6879-8614
Fax 81-6-6879-8616


Protein folding is a process in which an extended polypeptide chain acquires a unique folded conformation with biological activity. Clarifying the mechanism of protein folding is essential to improve our understanding of the structure and function of proteins. It is also important because many critical biological processes and disease states involve protein misfolding and aggregation reactions. We study the conformational stability and the mechanisms of protein folding and misfolding with various approaches including spectroscopies (NMR, fluorescence, CD), physicochemical measurements (calorimetry, analytical ultracentrifugation) and fluorescence microscopy. In addition, we are investigating the enhancing mechanism of the amyloid fibril formation by ultrasonication.

Fig. 1: Schematic presentation of folding pathway of bovine β-lactoglobulin


Fig. 2: The suggested models of FNR flexibility for function.
Fig. 3: An image of amyloid fibrils of amyloid-β peptide obtained using total internal reflection fluorescence microscopy.


Current Research Programs

  1. Observation of folding processes and clarification of the mechanism of protein folding
  2. Analysis of structural stability and dynamics of protein molecules
  3. Analysis of structural stability and the mechanism of formation of amyloid fibrils


  1. Ultrasonication-Dependent Acceleration of the Formation of Amyloid Fibrils. So et al. (2011) J Mol. Biol. 412, 568-77.
  2. A Binding Energetics of Ferredoxin-NADP+ Reductase with Ferredoxin and Its Relation to Function. Lee et al. (2011) ChemBioChem 12, 2062-2070.
  3. A Circumventing Role for the Non-Native Intermediate in the Folding of β-Lactoglobulin. Sakurai et al. (2011) Biochemistry 50, 6498-6507.
  4. Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions. Yanagi et al. (2011) J. Biol. Chem. 286, 23959-23966.
  5. Destruction of amyloid fibrils of keratoepithelin peptides by laser irradiation coupled with amyloid-specific thiofravin T. Ozawa et al. (2011) J. Biol. Chem., 286, 10856-10863