Structural fluctuations and functional expression of the chaperonin complexes

• Project Area: Molecular Science of Fluctuations toward Biological Functions
• Project/Area Number: 20107009
• Research Category: Grant-in-Aid for Scientific Research on Innovative Areas (Research in a proposed research area)
• Allocation Type: Single-year Grants
• Review Section: Science and Engineering
• Research Institution: National Institutes of Natural Sciences Okazaki Research Facilities
• Principal Investigator: KUWAJIMA Kunihiro 大学共同利用機関法人自然科学研究機構(岡崎共通研究施設), 岡崎統合バイオサイエンスセンター, 教授 (70091444)
• Co-Investigator(Renkei-kenkyūsha): MAKABE Koki 大学共同利用機関法人自然科学研究機構(岡崎共通研究施設), 岡崎統合バイオサイエンスセンター, 助教 (20508072)
• Project Period (FY): 2008 – 2012
• Project Status: Completed (Fiscal Year 2012)
• Budget Amount: ¥89,310,000 (Direct Cost: ¥68,700,000、Indirect Cost: ¥20,610,000); Fiscal Year 2012: ¥15,990,000 (Direct Cost: ¥12,300,000、Indirect Cost: ¥3,690,000); Fiscal Year 2011: ¥15,990,000 (Direct Cost: ¥12,300,000、Indirect Cost: ¥3,690,000); Fiscal Year 2010: ¥17,030,000 (Direct Cost: ¥13,100,000、Indirect Cost: ¥3,930,000); Fiscal Year 2009: ¥18,200,000 (Direct Cost: ¥14,000,000、Indirect Cost: ¥4,200,000); Fiscal Year 2008: ¥22,100,000 (Direct Cost: ¥17,000,000、Indirect Cost: ¥5,100,000)
• Keywords: 蛋白質 / フォールディング / 分子シャペロン / シャペロニン / 構造揺らぎ / 水素交換法 / 二次元NMR / 生物物理 / 分子機械 / 分子認識 / 生体分子 / アロステリック転移 / 分子シャペロニン

Research Abstract

The molecular chaperone is an important concept that connects a molecular-level biological process, protein folding, to cellular-level biological processes. In this project, we studied physicochemical relationships between structural fluctuations and functional expression of the chaperonin complexes. To elucidate how the biological functions utilize the structural fluctuations of the complexes, we investigated hydrogen/deuterium (H/D)-exchange reactions of the GroES portion of various chaperonin complexes by dimethylsulfoxide-quenched H/D-exchange two-dimensional NMR spectroscopy.

Research Products

• [Journal Article] NMR characterization of the interaction of GroEL with amyloid β as a model ligand. (2013)
  • Author(s): Yagi-Utsumi, M., Kunihara, T., Nakamura, T., Uekusa, Y., Makabe, K., Kuwajima, K. & Kato, K.
  • Journal Title: FEBS Lett. Volume: (In press)
  • Peer Reviewed
• [Journal Article] Molecular mechanisms of the cytotoxicity of human α-lactalbumin made lethal to tumor cells (HAMLET) and other protein-oleic acid complexes. (2013)
  • Author(s): Nakamura, T., Aizawa, T., Kariya, R., Okada, S., Demura, M., Kawano, K., Makabe, K. & Kuwajima, K.
  • Journal Title: J. Biol. Chem. Volume: 288 Pages: 14408-14416
  • Peer Reviewed
• [Journal Article] The H/D-Exchange Kinetics of the Escherichia coli Co-Chaperonin GroES Studied by 2D NMR and DMSO-Quenched Exchange Methods. (2013)
  • Author(s): Chandak, M.S., Nakamura, T., Makabe, K., Takenaka, T., Mukaiyama, A., Chaudhuri, T.K., Kato, K. & Kuwajima, K.
  • Journal Title: J. Mol. Biol. Volume: (In press)
  • Peer Reviewed
• [Journal Article] The use of spin desalting columns in DMSO-quenched H/D-exchange NMR experiments. (2013)
  • Author(s): Chandak, M.S., Nakamura, T., Takenaka, T., Chaudhuri, T.K., Yagi-Utsumi, M., Chen, J., Kato, K. & Kuwajima, K.
  • Journal Title: Protein Sci. Volume: 22 Pages: 486-491
  • Peer Reviewed
• [Journal Article] Structural insights into the stability perturbations induced by N-terminal variation in human and goat α-lactalbumin. (2013)
  • Author(s): Makabe, K., Nakamura, T. & Kuwajima, K.
  • Journal Title: Protein Eng. Des. Sel. Volume: 26 Pages: 165-170
  • Peer Reviewed
• [Journal Article] Native-state heterogeneity of β_2-microglobulin as revealed by kinetic folding and real-time NMR experiments. (2013)
  • Author(s): Mukaiyama, A., Nakamura, T., Makabe, K., Maki, K., Goto, Y. & Kuwajima, K.
  • Journal Title: J. Mol. Biol. Volume: 425 Pages: 257-272
  • Peer Reviewed
• [Journal Article] The molten globule of β_2-microglobulin accumulated at pH 4 and its role in protein folding. (2013)
  • Author(s): Mukaiyama, A., Nakamura, T., Makabe, K., Maki, K., Goto, Y. & Kuwajima, K.
  • Journal Title: J. Mol. Biol. Volume: 425 Pages: 273-291
  • Peer Reviewed
• [Journal Article] Nucleotide-induced conformational changes of tetradecameric GroEL mapped by H/D exchange monitored by FT-ICR mass spectrometry. (2013)
  • Author(s): Zhang, Q., Chen, J., Kuwajima, K., Zhang, H.M., Xian, F., Young, N.L. & Marshall, A.G.
  • Journal Title: Sci Rep Volume: 3 Pages: 1247-1247
  • Peer Reviewed
• [Journal Article] NMR characterization of interaction of GroEL with amyloid β as a model ligand. (2013)
  • Author(s): M.Yagi-Utsumi, T.Kunihara, T.Nakamura, Y.Uekusa, K.Makabe, K.Kuwajima, and K.Kato
  • Journal Title: FEBS Lett. Volume: 587 Issue: 11 Pages: 605-609
  • DOI: 10.1016/j.febslet.2013.04.007
  • Peer Reviewed
• [Journal Article] The H/D-exchange Kinetics of the Escherichia coli Co-chaperonin GroES Studied by 2D-NMR and DMSO-Quenched Exchange Methods. (2013)
  • Author(s): Chandak MS, Nakamura T, Makabe K, Takenaka T, Mukaiyama A, Chaudhuri TK, Kato K, Kuwajima K.
  • Journal Title: J Mol Biol. Volume: 425 Issue: 14 Pages: 2541-2560
  • DOI: 10.1016/j.jmb.2013.04.008
  • Peer Reviewed
• [Journal Article] Molecular mechanisms of the cytotoxicity of human α-lactalbumin made lethal to tumor cells (HAMLET) and other protein-oleic acid complexes. (2013)
  • Author(s): Nakamura, Takashi
  • Journal Title: J. Biol. Chem. Volume: -
  • Peer Reviewed
• [Journal Article] Nucleotide-induced conformational changes of tetradecameric GroEL mapped by H/D exchange monitored by FT-ICR mass spectrometry. (2013)
  • Author(s): Zhang, Qian
  • Journal Title: Sci. Rep. Volume: 3 Issue: 1 Pages: 1247-1247
  • DOI: 10.1038/srep01247
  • Peer Reviewed
• [Journal Article] The molten globule of β(2)-microglobulin accumulated at pH 4 and its role in protein folding (2013)
  • Author(s): A. Mukaiyama, T. Nakamura, K. Makabe, K. Maki, Y. Goto, K. Kuwajima
  • Journal Title: J. Mol. Biol. Volume: 425 Issue: 2 Pages: 273-291
  • DOI: 10.1016/j.jmb.2012.11.002
  • Peer Reviewed
• [Journal Article] Native-state heterogeneity of β(2)-microglobulin as revealed by kinetic folding and real-time NMR experiments. (2013)
  • Author(s): Mukaiyama A, Nakamura T, Makabe K, Maki K, Goto Y, Kuwajima K.
  • Journal Title: J Mol Biol. Volume: 425 Issue: 2 Pages: 257-272
  • DOI: 10.1016/j.jmb.2012.11.004
  • Peer Reviewed
• [Journal Article] Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperone. (2012)
  • Author(s): Chen, J., Yagi, H., Sormanni, P., Vendruscolo, M., Makabe, K., Nakamura, T., Goto, Y. & Kuwajima, K.
  • Journal Title: FEBS Lett. Volume: 586 Pages: 1120-1127
  • Peer Reviewed
• [Journal Article] Sequential four-state folding/unfolding of goat α-lactalbumin and its N-terminal variants. (2012)
  • Author(s): Tomoyori, K., Nakamura, T., Makabe, K., Maki, K., Saeki, K. & Kuwajima, K.
  • Journal Title: Proteins Volume: 80 Pages: 2191-2206
  • Peer Reviewed
• [Journal Article] Fibrillogenic propensity of the GroEL apical domain : A Janus-faced minichaperone (2012)
  • Author(s): Chen, Jin
  • Journal Title: FEBS Letters Volume: VOL.13(印刷中)(未定)
  • Peer Reviewed
• [Journal Article] Dissecting a bimolecular process of MgATP^<2-> binding to the chaperonin GroEL. (2011)
  • Author(s): Chen, J., Makabe, K., Nakamura, T., Inobe, T. & Kuwajima, K.
  • Journal Title: J. Mol. Biol. Volume: 410 Pages: 343-356
  • Peer Reviewed
• [Journal Article] Solubilization and folding of a fully active recombinant Gaussia luciferase with native disulfide bonds by using a SEP-Tag. (2011)
  • Author(s): Rathnayaka, T., Tawa, M., Nakamura, T., Sohya, S., Kuwajima, K., Yohda, M. & Kuroda, Y.
  • Journal Title: Biochim. Biophys. Acta Volume: 1814 Pages: 1775-1778
  • Peer Reviewed
• [Journal Article] Solubilization and folding of a fully active recombinant Gaussia luciferase with native disulfide bonds bv using a SEP-Tag (2011)
  • Author(s): Rathnayaka, T.
  • Journal Title: Biochim Biophys Acta Volume: 1814 Pages: 1774-1778
  • Peer Reviewed
• [Journal Article] Dissecting a bimolecular process of MgATP^2- binding to the chaperonin GroEL. (2011)
  • Author(s): Chen, J., Makabe, K., Nakamura, T., Inobe, T., Kuwajima, K.
  • Journal Title: J.Mol.Biol. in the press.
  • Peer Reviewed
• [Journal Article] Dissecting a bimolecular process of MgATP^<2-> binding to the chaperonin GroEL (2011)
  • Author(s): Jin Chen
  • Journal Title: J.Mol.Biol. Volume: (印刷中)
  • Peer Reviewed
• [Journal Article] Adaptation of a hyperthermophilic group II chaperonin to relatively moderate temperatures. (2010)
  • Author(s): Kanzaki, T., Ushioku, S., Nakagawa, A., Oka, T., Takahashi, K., Nakamura, T., Kuwajima, K., Yamagishi, A. & Yohda, M.
  • Journal Title: Protein Eng. Des. Sel. Volume: 23 Pages: 393-402
  • Peer Reviewed
• [Journal Article] Different folding pathways taken by highly homologous proteins, goat α-lactalbumin and canine milk lysozyme. (2010)
  • Author(s): Nakamura, T., Makabe, K., Tomoyori, K., Maki, K., Mukaiyama, A. & Kuwajima, K.
  • Journal Title: J. Mol. Biol. Volume: 396 Pages: 1361-1378
  • Peer Reviewed
• [Journal Article] Flexible recognition of the tRNA G18 methylation target site by TrmH methyltransferase through first binding and induced fit processes. (2010)
  • Author(s): Ochi, A., Makabe, K., Kuwajima, K. & Hori, H.
  • Journal Title: J. Biol. Chem. Volume: 285 Pages: 9018-9029
  • Peer Reviewed
• [Journal Article] Different folding pathways taken by highly homologous proteins, goat α-lactalbumin and canine milk lysozyme. (2010)
  • Author(s): Nakamura, T., Makabe, K., Tomoyori, K., Maki, K., Mukaiyama, A., Kuwajima, K.
  • Journal Title: J.Mol.Biol. 396 Pages: 1361-1378
  • Peer Reviewed
• [Journal Article] 何がタンパク質のフォールディング経路を決めるのか? (2010)
  • Author(s): 中村敬
  • Journal Title: MedicalBio(オーム社) Volume: 10月号別冊 Pages: 49-54
• [Journal Article] Flexible recognition of the tltNA G18 methylation target site by TrmH methyltransferase through first binding and induced fit processes (2010)
  • Author(s): A.Ochi
  • Journal Title: J.Biol.Chem. Pages: 9018-9029
  • Peer Reviewed
• [Journal Article] Adaptation of a hyperthermophilic group II chaperonin to relatively moderate temperatures (2010)
  • Author(s): T.Kanzaki
  • Journal Title: Pmtein.Eng.Des.Sel. 23 Pages: 393-402
  • Peer Reviewed
• [Journal Article] Different folding pathways taken by highly homologous proteins, goat α-lactalbumin and canine milk lysozyme (2010)
  • Author(s): T.Nakamura
  • Journal Title: J.Mol.Biol. 396 Pages: 1361-1378
  • Peer Reviewed
• [Journal Article] Non-native alpha-helix formation is not necessary for folding of lipocalin: comparison of burst-phase folding between tear lipocalin and β-lactoglobulin. (2009)
  • Author(s): Tsukamoto, S., Yamashita, T., Yamada, Y., Fujiwara, K., Maki, K., Kuwajima, K., Matsumura, Y., Kihara, H., Tsuge, H. & Ikeguchi, M.
  • Journal Title: Proteins Volume: 76 Pages: 226-236
  • Peer Reviewed
• [Journal Article] Non-native α-helix formation is not necessary for folding of lipocalin : Comparison of burst-phase folding between tear lipocalin and β-lactoglobulin. (2009)
  • Author(s): Tsukamoto, S., Yamashita, T., Yamada, Y., Fujiwara, K., Maki, K., Kuwajima, K., Matsumura, Y., Kihara, H., Tsuge, H., Ikeguchi, M.
  • Journal Title: Proteins 76 Pages: 226-236
  • Peer Reviewed
• [Journal Article] Non-native α-helix fbmlation is not necessary for folding of lipocalin : comparison of burst-phase folding between tear lipocalin and β-lactoglobulin (2009)
  • Author(s): S.Tsukamoto
  • Journal Title: Proteins 76 Pages: 226-236
  • Peer Reviewed
• [Journal Article] Non-native α-helix formation is not necessary for folding of lipocalin : Comparison of burst-phase folding between tear lipocalin and β-lactoglobulin (2009)
  • Author(s): S. TSUKAMOTO
  • Journal Title: Proteins (掲載確定 印刷中)
  • Peer Reviewed
• [Journal Article] Asymmetry of the GroEL-GroES complex under physiological conditions as revealed by small-angle X-ray scattering. (2008)
  • Author(s): Inobe, T., Takahashi, K., Maki, K., Enoki, S., Kamagata, K., Kadooka, A., Arai, M. & Kuwajima, K.
  • Journal Title: Biophys. J. Volume: 94 Pages: 1392-1402
  • Peer Reviewed
• [Journal Article] Probing force-induced unfolding intermediates of a single staphylococcal nuclease molecule and the effect of ligand binding. (2008)
  • Author(s): Ishii, T., Murayama, Y., Katano, A., Maki, K., Kuwajima, K. & Sano, M.
  • Journal Title: Biochem. Biophys. Res. Commun. Volume: 375 Pages: 586-591
  • Peer Reviewed
• [Journal Article] Sequential action of ATP-dependent subunit conformational change and interaction between helical protrusions in the closure of the built-in lid of group II chaperonins. (2008)
  • Author(s): Kanzaki, T., Iizuka, R., Takahashi, K., Maki, K., Masuda, R., Sahlan, M., Yebenes, H., Valpuesta, J.M., Oka, T., Furutani, M., Ishii, N., Kuwajima, K. & Yohda, M.
  • Journal Title: J. Biol. Chem. Volume: 283 Pages: 34773-34784
  • Peer Reviewed
• [Journal Article] Asymmetry of the GroEL-GroES complex under physiological conditions as revealed by small-angle X-ray scattering. (2008)
  • Author(s): Inobe, T., Takahashi, K., Maki, K., Enoki, S., Kamagata, K., Kadooka, A., Arai, M., Kuwajima, K.
  • Journal Title: Biophys.J. 94 Pages: 1392-1402
  • Peer Reviewed
• [Journal Article] Probing force- induced unfolding intermediates of a single staphylococcal nuclease molecule and the effect of ligand binding. (2008)
  • Author(s): Ishii, T., Murayama, Y., Katano, A., Maki, K., Kuwajima, K., Sano, M.
  • Journal Title: Biochem.Biophys.Res.Commun. 375 Pages: 586-591
  • Peer Reviewed
• [Journal Article] Sequential Action of ATP-dependent Subunit Conformational Change and Interaction between Helical Protrusions in the Closure of the Built-in Lid of Group II Chaperonins (2008)
  • Author(s): T. KANZAKI
  • Journal Title: J. Biol. Chem. 283 Pages: 34773-34784
  • Peer Reviewed
• [Journal Article] Probing force-induced unfolding intermediates of a single staphylococcal nuclease molecule and the effect of ligand binding (2008)
  • Author(s): T. ISHII
  • Journal Title: Biochem. Biophys. Res. Commun. 375 Pages: 586-591
  • Peer Reviewed
• [Presentation] Sequential four-state folding/unfolding of goat α-lactalbumin and its N-terminal variants (2013)
  • Author(s): 桑島邦博
  • Organizer: 17th Hiroshima International Symposium on Synchrotron Radiation - Progress in materials science and synchrotron radiation -
  • Place of Presentation: 広島県東広島市・広島大学・広島大学学士会館
  • Year and Date: 2013-02-28
  • Invited
• [Presentation] Sequential four-state folding/unfolding of goat α-lactalbumin and its N-terminal variants (2013)
  • Author(s): 桑島邦博
  • Organizer: 5ｔｈ Korea-Japan Seminar on Biommolecular Sciences- Experiments and Simulations
  • Place of Presentation: 韓国、High1リゾート
  • Year and Date: 2013-02-24
  • Invited
• [Presentation] Sequential four-state folding/unfolding of goat α-lactalbumin and its N-terminal variants. (2013)
  • Author(s): Kuwajima, K.
  • Organizer: 17th Hiroshima International Symposium on Synchrotron Radiation - Progress in materials science and synchrotron radiation -
  • Place of Presentation: Hiroshima Univ.
• [Presentation] Structural fluctuation of free GroES and the GroES-SR1 complex studied by the use of hydrogen/deuterium (H/D) exchange. (2013)
  • Author(s): Chandak, M.S., Nakamura, T., Makabe, K., Takenaka, T., Mukaiyama, A., Chaudhuri, T.K., Chen, J., Kato, K. & Kuwajima, K.
  • Organizer: 57th Annual Meeting of the Biophysical Society (USA)
  • Place of Presentation: Philadelphia, USA
• [Presentation] The structure and function of HAMLET and its related protein complexes (2012)
  • Author(s): 桑島邦博
  • Organizer: 3rd HAMLET Conference
  • Place of Presentation: スウェーデン、ルンド
  • Year and Date: 2012-12-07
  • Invited
• [Presentation] Structural fluctuations and functional expression of the chaperonin complexes (2012)
  • Author(s): 桑島邦博
  • Organizer: 6th International Symposium "Molecular Science of Fluctuations toward Biological Functions"
  • Place of Presentation: 京都府京都市・京都テルサ
  • Year and Date: 2012-12-05
  • Invited
• [Presentation] シャペロニン超分子複合体の水素交換反応 (2012)
  • Author(s): 桑島邦博
  • Organizer: 大阪大学蛋白質研究所セミナー「分子シャペロンの機能発現の新展開と細胞制御」
  • Place of Presentation: 大阪府吹田市・大阪大学・蛋白質研究所・講堂
  • Year and Date: 2012-11-15
  • Invited
• [Presentation] Molecular mechanisms of cytotoxicity of HAMLET and other protein-oleic acid complexes (2012)
  • Author(s): 桑島邦博
  • Organizer: 12th KIAS Conference on Protein Structure
  • Place of Presentation: 韓国、ソウル
  • Year and Date: 2012-10-11
  • Invited
• [Presentation] Molecular mechanisms of cytotoxicity of HAMLET and other protein-oleic acid complexes (2012)
  • Author(s): 桑島邦博
  • Organizer: IGER International Symposium on Science of Molecular Assembly and Biomolecular Systems 2012
  • Place of Presentation: 愛知県名古屋市・名古屋大学・野依記念学術交流館
  • Year and Date: 2012-09-04
  • Invited
• [Presentation] To What Extent Has the Problem of Protein Folding Been Solved? (2012)
  • Author(s): 桑島邦博
  • Organizer: 第12回日本蛋白質科学会ワークショップ「タンパク質のフォールディング問題はどこまで解決されたか」
  • Place of Presentation: 愛知県名古屋市・名古屋国際会議場
  • Year and Date: 2012-06-20
  • Invited
• [Presentation] The structure and function of HAMLET and its related protein complexes. (2012)
  • Author(s): Kuwajima, K.
  • Organizer: 3rd HAMLET Conference
  • Place of Presentation: Lund, Sweden
• [Presentation] Structural fluctuations and functional expression of the chaperonin complexes. (2012)
  • Author(s): Kuwajima, K.
  • Organizer: 6th International Symposium "Molecular Science of Fluctuations toward Biological Functions,"
  • Place of Presentation: Kyoto, Japan
• [Presentation] シャペロニン超分子複合体の水素交換反応 (2012)
  • Author(s): 桑島邦博
  • Organizer: 大阪大学蛋白質研究所セミナー「分子シャペロンの機能発現の新展開と細胞制御」
  • Place of Presentation: 大阪
• [Presentation] Molecular Mechanisms of the Escherichia coli Chaperonin Function. (2011)
  • Author(s): Kuwajima, K.
  • Organizer: 3rd Asia Pacific Protein Association (APPA) Conference
  • Place of Presentation: Shanghai, China
• [Presentation] Molecular Mechanisms of the Escherichia coli Chaperonin Function (2011)
  • Author(s): 桑島邦博
  • Organizer: The 3rd Asia Pacific Protein Association (APPA) Conference
  • Place of Presentation: 上海大学(中国)(招待講演)
• [Presentation] Molecular mechanisms of the Escherichia coli chanperonin function (2011)
  • Author(s): K.Kuwajima
  • Organizer: 3rd APPA Conference
  • Place of Presentation: Shanghai University,Shanghai,China
• [Presentation] Identification of fatty-acid binding site in the anti-tumor complex of of α-lactalbuin by 920-MHz NMR spectroscopy (2010)
  • Author(s): K.Kuwajima
  • Organizer: IPR Seminar "Cooperation in Protein Science between Asian and Pacific Countries"
  • Place of Presentation: the Institute for Protein Research, Osaka University(大阪)
  • Year and Date: 2010-06-14
• [Presentation] Identification of fatty-acid binding site in the anti-tumor complex of of α-lactalbuin by 920-MHz NMR spectroscopy (2010)
  • Author(s): K.Kuwajima
  • Organizer: The 10th KIAS Conference on Protein Structure and Function
  • Place of Presentation: Korea Institute for Advanced Study(KIAS)Seoul,Korea
• [Presentation] Is the Folding Pathway Conserved in Homologous Proteins (2010)
  • Author(s): K.Kuwajima
  • Organizer: Bit Life Science's 3rd Annual Protein and Peptide Conference After a Solution of the Machines of Life
  • Place of Presentation: Beijing International Convention Center,Beijing,China
• [Presentation] Molecular mechanisms of protein folding (2010)
  • Author(s): K.Kuwajima
  • Organizer: 2010 Annual Meeting of Asian CORE Program Frontiers of Materials,Photo-,and Theoretical Molecular Sciences Insitute of Atomic and Molecular Sciences
  • Place of Presentation: Academia Sinica,Taipei,Taiwan
• [Presentation] Identification of fatty-acid binding site in the anti-tumor complex of of α-lactalbuin by 920-MHz NMR spectroscopy (2010)
  • Author(s): K.Kuwajima
  • Organizer: The 10th KIAS Conference on Protein Structure and Function
  • Place of Presentation: Korea Institute for Advanced Study, Seoul, Korea
• [Presentation] Molecular Mechanisms of Protein Folding (2010)
  • Author(s): K.Kuwajima
  • Organizer: The Overseas Sokendai Lecture in Bangkok FY2010 & The Inaugural CU-IMS Joint Symposium
  • Place of Presentation: Chulalongkorn University, Bangkok, Thailand
• [Presentation] Moleculaz Mechanisms of Protein Folding (2010)
  • Author(s): K.Kuwajima
  • Organizer: 2010 Annual Meeting of Asian CORE Program "Frontiers of Materials, Photo-, and Theoretical Molecular Sciences"
  • Place of Presentation: Institute of Atomic and Molecular Sciences, Academia Sinica, Taiwan
• [Presentation] Is the folding pathway conserved in homologous proteins? (2010)
  • Author(s): K.Kuwajima
  • Organizer: PepCon-2010
  • Place of Presentation: Beijing Intemational Convention Center, China
• [Presentation] Hydrogen-exchange kinetics of the Fscherichia coli chaperonin complex (2009)
  • Author(s): K,Kuwajima
  • Organizer: Japan-Korea Symposium on Molecular Science 2009 "Chemical Dynamics in Materials and Biological Molecular Sciences"
  • Place of Presentation: Awaji Yumebutai IntemationalConference Center, Awajishima, Japan
• [Presentation] A minor component of native β2-microglobulin and its relationship to dialysis-related amyloidosis (2009)
  • Author(s): K.Kuwajima
  • Organizer: The 9th KIAS-SNU Conference on Protein Structure and Function, Seoul National University
  • Place of Presentation: Seoul National University, Seoul, Korea
• [Presentation] Hydrogen-exchange kinetics of the Escherichia coli chaperonin complex (2009)
  • Author(s): K.Kuwajima
  • Organizer: 2nd Japan-Korea Seminar on Biomolecular Sciences-Experiments and Simulations
  • Place of Presentation: Nagoya University, Nagoya, Japan
• [Presentation] Molecular Mechanisms of the Chaperone Function of GroEL (2008)
  • Author(s): 桑島 邦博
  • Organizer: 8th KIAS-Yonsei Conference on Protein Structure and Function
  • Place of Presentation: Seoul, Korea
  • Year and Date: 2008-10-11
• [Presentation] Folding Mechanisms of Homologous Proteins : A Comparative Study between Lysozyme and α-Lactalbumin (2008)
  • Author(s): 桑島 邦博
  • Organizer: ACS 236^<th> National Meeting Symposium
  • Place of Presentation: Philadelphia, U. S. A.
  • Year and Date: 2008-08-21
• [Book] Water and Biomolecules-Physical Chemistry of Life Phenomena (分担執筆) (2009)
  • Author(s): Kuwajima, K.
  • Total Pages: 307
  • Publisher: Springer-Verlag, Berlin & Heidelberg
• [Book] Water and Biomolecules-Physical Chemistry of Life Phenomena.(Kuwajima.K, Goto.Y, Hirata.F, Kataoka.M., Terazima.M, Eds.)(A.Experimental and Simulation Studies of the Folding/Unfolding of Goat α-Lactalbumin.) (2009)
  • Author(s): Kuwajima, K., Oroguchi, T., Nakamura, T., Ikeguchi, M., Kidera
  • Publisher: Springer-Verlag.Berlin Heiderberg
• [Book] Water and Biomolecules-Physical Chemistry of Life Phenomena (2009)
  • Author(s): K. Kuwajima
  • Total Pages: 307
  • Publisher: Springer-Verlag, Berlin & Heidelberg
• [Remarks]
  • URL: http://researchmap.jp/read0007744/
• [Remarks]
  • URL: http://gagliano.ims.ac.jp/Welcome.html
• [Remarks]
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• [Patent(Industrial Property Rights)] 蛋白質-化学療法剤複合体及びその製造方法,並びに医薬 (2012)
  • Inventor(s): 桑島邦博、中村敬、真壁幸樹、岡田誠治
  • Industrial Property Rights Holder: 自然科学研究機構、熊本大学
  • Industrial Property Number: 2012-147492
  • Filing Date: 2012-06-29
• [Patent(Industrial Property Rights)] 蛋白質―化学療法剤複合体及びその製造方法，並びに医薬 (2012)
  • Inventor(s): 桑島邦博
  • Industrial Property Rights Holder: 桑島邦博
  • Industrial Property Rights Type: 特許
  • Industrial Property Number: 2012-147492
  • Filing Date: 2012-06-29
• [Patent(Industrial Property Rights)] 球状蛋白質の準安定状態を用いた抗癌細胞作用のある分子の作成 (2011)
  • Inventor(s): 桑島邦博、中村敬、真壁幸樹
  • Industrial Property Rights Holder: 自然科学研究機構
  • Industrial Property Number: 2011-238611
  • Filing Date: 2011-10-31
• [Patent(Industrial Property Rights)] 球状蛋白質の準安定状態を用いた抗癌細胞作用のある分子の作成 (2011)
  • Inventor(s): 桑島邦博, 中村敬, 真壁幸樹
  • Industrial Property Rights Holder: 自然科学研究機構
  • Industrial Property Number: 2011-238611
  • Filing Date: 2011-10-31