藤原 和夫

生体生命情報学、構造生物化学、生物物理学

タンパク質複合体構造解析

物理化学実験、物理化学実習、プログラミング演習Ⅰ・Ⅱ、プロジェクト・スタディーズA・B、ケーススタディⅠ・Ⅱ、演習Ⅰ・Ⅱ

蛋白質設計学、生物物理学

• タンパク質のアミノ酸配列と立体構造に関する統計的解析
• タンパク質の立体構造形成機構に関する実験的解析

生体高分子特論

1974年　富山県生まれ
2001年　創価大学大学院博士課程修了　博士（工学）
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2001年　株式会社ヒューリンクス
2005年　創価大学工学部生命情報工学科　講師
2013年　創価大学工学部生命情報工学科　准教授

• 日本生物物理学会
• 日本蛋白質科学会

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.

生体生命情報学、構造生物化学、生物物理学

タンパク質複合体構造解析