- 教員一覧
- 藤原 和夫
藤原 和夫（准教授）
フジワラ カズオ
| 専門分野 | 生体生命情報学、構造生物化学、生物物理学 |
|---|---|
| 担当科目 | 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 |
| 研究テーマ | タンパク質複合体構造解析 |
理工学研究科 生命理学専攻
専門分野 蛋白質設計学、生物物理学 担当科目 生体高分子特論 研究テーマ ・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略歴 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 准教授主な著書論文 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.所属学会 ・日本生物物理学会
・日本蛋白質科学会
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