Associate Professor

Kazuo Fujiwara

Profile

Specialized field

Bioinformatics, Structural Biochemistry, Biophysics

Research theme

Protein complex structure analysis

Subjects in charge

Physical chemistry experiments, physical chemistry training, programming exercises I and II, project studies A and B, case studies I and II, exercises I and II

Specialized field

Protein design, biophysics

Research theme
  • Statistical analysis of protein amino acid sequences and three-dimensional structures
  • Experimental analysis of the mechanism of protein conformation
Subjects in charge

Special Lecture on Biopolymers

Main career, work history, and academic background

Born in Toyama Prefecture in 1974
2001: Completed doctoral course at Soka University Graduate School, Ph.D. (Engineering)
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2001 Hulinks Co., Ltd.
2005 Lecturer Department of Bioinformatics, Faculty of Engineering, Soka University
2013: Associate Professor, Department of Bioinformatics, Faculty of Engineering, Soka University

Affiliated academic societies and organizations
  • Biophysical Society of Japan
  • Protein Science Society of Japan
Main Papers and Publications
  1. Sato D, Takebe S, Kurobe A, Ohtomo H, Fujiwara K, Ikeguchi M.
    Electrostatic Repulsion during Ferritin Assembly and Its Screening by Ions.
    Biochemistry. 2016 Jan 26;55(3):482-8.
  2. Sato D, Ohtomo H, Yamada Y, Hikima T, Kurobe A, Fujiwara K, Ikeguchi M.
    Ferritin Assembly Revisited: A Time-Resolved Small-Angle X-ray Scattering Study.
    Biochemistry. 2016 Jan 19;55(2):287-93.
  3. Fujiwara K, Ebisawa S, Watanabe Y, Fujiwara H, Ikeguchi M.
    The origin of β-strand bending in globular proteins.
    BMC Struct Biol. 2015 Oct 22;15:21.
  4. Ohtomo H, Ohtomo M, Sato D, Kurobe A, Sunato A, Matsumura Y, Kihara H, Fujiwara K, Ikeguchi M.
    A Physicochemical and Mutational Analysis of Intersubunit Interactions of Escherichia coli Ferritin A.
    Biochemistry. 2015 Oct 13;54(40):6243-51.
  5. Okabe T, Miyajima T, Nakagawa K, Tsukamoto S, Fujiwara K, Ikeguchi M.
    Effect of non-native helix destabilization on the folding of equine β-lactoglobulin.
    J Biochem. 2014 Nov;156(5):291-7.
  6. Okabe T, Tsukamoto S, Fujiwara K, Shibayama N, Ikeguchi M.
    Delineation of solution burst-phase protein folding events by encapsulating the proteins in silica gels.
    Biochemistry. 2014 Jun 17;53(23):3858-66.
  7. Fujiwara K, Ebisawa S, Watanabe Y, Toda H, Ikeguchi M.
    Local sequence of protein β-strands influences twist and bend angles.
    Proteins. 2014 Jul;82(7):1484-93.
  8. Nakagawa K, Yamada Y, Matsumura Y, Tsukamoto S, Yamamoto-Ohtomo M, Ohtomo H, Okabe T, Fujiwara K, and Ikeguchi M.
    Relationship between chain collapse and secondary structure formation in a partially folded protein.
    Biopolymers. 2014 Jun;101(6):651-8.
  9. Fujiwara K, Toda H, Ikeguchi M.
    Dependence of alpha-helical and beta-sheet amino acid propensities on the overall protein fold type.
    BMC Struct Biol. 2012 Aug 2;12:18.
  10. Ohtomo H, Fujiwara K, Ikeguchi M.
    Important Role of Methionine 145 in Dimerization of Bovine β-Lactoglobulin.
    J Biochem. 2012 Mar;151(3):329-34.
  11. Yamamoto M, Nakagawa K, Fujiwara K, Shimizu A, Ikeguchi M, Ikeguchi M.
    A native disulfide stabilizes non-native helical structures in partially folded states of equine β-lactoglobulin.
    Biochemistry. 2011 Dec 13;50(49):10590-7.
  12. Tsukamoto S, Fujiwara K, Ikeguchi M.
    Fatty acids bound to recombinant tear lipocalin and their role in structural stabilization.
    J Biochem. 2009 Sep;146(3):343-50.
  13. Tsukamoto S, Yamashita T, Yamada Y, Fujiwara K, Maki K, Kuwajima K, Matsumura Y, Kihara H, Tsuge H, Ikeguchi M.
    Non-native alpha-helix formation is not necessary for folding of lipocalin: Comparison of burst-phase folding between tear lipocalin and beta-lactoglobulin.
    Proteins. 2009 Jul;76(1):226-36.
  14. Fujiwara K, Ikeguchi M.
    OLIGAMI: OLIGomer Architecture and Molecular Interface.
    The Open Bioinformatics Journal, 2008, 2, 50-53.
  15. Nakagawa K, Yamada Y, Fujiwara K, Ikeguchi M.
    Interactions Responsible for Secondary Structure Formation during Folding of Equine beta-Lactoglobulin.
    J Mol Biol. 2007 April 6;367(4):1205-1214.
  16. Nakagawa K, Tokushima A, Fujiwara K, Ikeguchi M.
    Proline Scanning Mutagenesis Reveals Non-Native Fold in the Molten Globule State of Equine beta-Lactoglobulin.
    Biochemistry. 2006 Dec 26;45(51):15468-15473.
  17. Yamada Y, Nakagawa K, Yajima T, Saito K, Tokushima A, Fujiwara K, Ikeguchi M.
    Structural and thermodynamic consequences of removal of a conserved disulfide bond from equine beta-lactoglobulin.
    Proteins. 2006 May 15;63(3):595-602.
  18. Yamada Y, Yajima T, Fujiwara K, Arai M, Ito K, Shimizu A, Kihara H, Kuwajima K, Amemiya Y, Ikeguchi M.
    Helical and Expanded Conformation of Equine beta-Lactoglobulin in the Cold-denatured State.
    J Mol Biol. 2005 Jul 8;350(2):338-48.
  19. Fujiwara K, Ikeguchi M, Sugai S.
    A partially unfolded state of equine beta-lactoglobulin at pH 8.7.
    J Protein Chem. 2001 Feb;20(2):131-7.
  20. Fujiwara K, Arai M, Shimizu A, Ikeguchi M, Kuwajima K, Sugai S.
    Folding-unfolding equilibrium and kinetics of equine beta-lactoglobulin: equivalence between the equilibrium molten globule state and a burst-phase folding intermediate.
    Biochemistry. 1999 Apr 6;38(14):4455-63.
Specialized field

Bioinformatics, Structural Biochemistry, Biophysics

Research theme

Protein complex structure analysis