西村 千秋
Faculty

学部・大学院

西村 千秋

所属 薬学部 薬学科 教授
最終学歴 東京大学大学院薬学系研究科 生命薬学専攻 博士課程修了
現在所属している学会 日本核磁気共鳴学会、日本薬学会、日本物理学会、日本生物物理学会、日本蛋白質科学会、横浜NMR学会
学士・修士・博士 薬学博士
所有資格
研究の分野 蛋白質の構造、構造形成、天然変性蛋白質、 薬学6802物理系薬学(A)物理化学(D)生物物理化学(H)構造生物学、複合化学4703高分子化学(G)高分子構造(K)生体関連高分子、4706生体関連化学(B)生体関連高分子化学
主な研究項目 核磁気共鳴(NMR)を用いた蛋白質の構造形成に関する研究、抗ウイルス薬のデザイン、天然変性蛋白質とアミロイド蛋白質の構造に関する研究
主な研究業績 Non-native alpha-helices in the initial folding intermediate facilitate the ordered assembly of the beta-barrel in beta-lactoglobulin/Biochemistry 56, 4799-4807, 2017/共著/2017.08
Folding of apomyoglobin: Analysis of transient intermediate structure during refolding using quick hydrogen deuterium exchange and NMR/Proc. Jpn. Acad., Ser. B, 93, 10-27, 2017/単著/2017.01
Effect of Glu12-His89 Interaction on Dynamic Structures in HIV-1 p17 Matrix Protein Elucidated by NMR/PLoS One 11, e0167176, 2016/共著/2016.12
アゾベンゼンの双方向光異性化反応を用いた高分子の構造相関NMR法/分光研究、258-260、2016/共著/2016.05
Structure-Correlation NMR Spectroscopy for Macromolecules Using Repeated Bidirectional Photoisomerization of Azobenzene/Anal. Chem. 87, 11544-11552, 2015/共著/2015.11
Comparison of residual alpha- and beta-structures between two intrinsically disordered proteins by using NMR/Biochim. Biophys. Acta 1854, 229-238, 2015/共著/2015.03
Long-range effects of tag sequence on marginally stabilized structure in HIV-1 p24 capsid protein monitored using NMR/Biochim. Biophys. Acta 1844, 1638-1647, 2014/共著/2014.09
Probing the non-native H helix translocation in apomyoglobin folding intermediates/Biochemistry 53, 3767-3780, 2014/共著/2014.06
Flexible and rigid structures in HIV-1 p17 matrix protein monitored by relaxation and amide proton exchange with NMR/Biochim. Biophys. Acta 1844, pp520-526, 2014/共著/2014.03
Remaining structures at the N- and C-terminal regions of alpha-synuclein accurately elucidated by amide-proton exchange NMR with fitting/FEBS Lett. 587, pp3709-3714, 2013/共著/2013.11
Consequence of stabilizing the natively disordered F helix for the folding pathway of apomyoglobin/J. Mol. Biol. 411, 248-263, 2011/共著/2011.05
Energetic frustration of apomyoglobin folding: role of the B helix/J. Mol. Biol. 396, pp.1319~1328, 2010/共著/2010.01
蛋白質は折りたたまなければ始まらない?/共立出版社、蛋白質核酸酵素/単著/2009.05
The kinetic and equilibrium molten globule intermediates of apoleghemoglobin differ in structure./J. Mol.Biol. 378, pp.715~725, 2008       /共著/2008.01
Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H/D exchange coupled with 2D NMR./Proc. Natl. Acad. Sci. USA 105, pp.13859~13864, 2008   /共著/2008.01
Disulfide-linked bovine beta-lactoglobulin dimers fold slowly navigating a glassy folding landscape./Biochemistry, 47, pp.5996~6006, 2008   /共著/2008.01
Identification of native and non-native structure in kinetic folding intermediates of apomyoglobin./J. Mol. Biol. 355, pp.139~156, 2006       /共著/2006.01
Sequence determinants of a protein folding pathway/J. Mol. Biol. 351, pp.383~392, 2005               /共著/2005.01
Enhanced picture of protein-folding intermediates using organic solvents in H/D exchange and quench-flow experiments/Proc. Natl. Acad. Sci. USA 102, pp.4765~4770, 2005       /共著/2005.01
Role of the B helix in early folding events in apomyoglobin: Evidence from site-directed mutagenesis for native-like long range interactions./J. Mol. Biol. 334, pp.293~307, 2003                /共著/2003.01
The apomyoglobin folding pathway revisited: Structural heterogeneity in the kinetic burst phase intermediate./J. Mol.Biol. 322, pp.483~489, 2002         /共著/2002.01
Conformational and dynamic characterization of the molten globule state of an apomyoglobin mutant with an altered folding pathway/Biochemistry 40, pp.14459~14467, 2001/共著/2001.01
Effect of salt on the stability and folding of staphylococcal nuclease./Biochemistry 40, pp.2113~2128,2001/共著/2001.01
Conservation of folding pathways in evolutionarily distant globin sequences./Nature Struct. Biol. 7, pp.679~686, 2000/共著/2000.01
Fluorence energy transfer indicates similar transient and equilibrium intermediates in staphylococcal nuclease folding/J. Mol. Biol. 299, pp.1133~1146, 2000/共著/2000.01
Changes in the apomyoglobin folding pathway caused by mutation of the distal histidine residue./Biochemistry 39, pp.11227~11237, 2000/共著/2000.01
主な担当授業科目名 卒業研究、薬学臨床実習2、アドバンスセミナー3