論文- 小井川 浩之 -
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件数:15件
[2018]
1.Microsecond resolved single-molecule FRET time series measurements based on the line confocal optical system combined with hybrid photodetectors.[Physical Chemistry Chemical Physics,20(5),(2018),3277-3285]Oikawa H, Takahashi T, Kamonprasertsuk S, Takahashi S.
10.1039/c7cp06268k
[2017]
2.Highly Heterogeneous Nature of the Native and Unfolded States of the B Domain of Protein A Revealed by Two-Dimensional Fluorescence Lifetime Correlation Spectroscopy.[Journal of Physical Chemistry B,121(22),(2017),5463-5473]Otosu T, Ishii K, Oikawa H, Arai M, Takahashi S, Tahara T.
10.1021/acs.jpcb.7b00546
[2016]
3.Significant Heterogeneity and Slow Dynamics of the Unfolded Ubiquitin Detected by the Line Confocal Method of Single-Molecule Fluorescence Spectroscopy.[Journal of Physical Chemistry B,120(34),(2016),8818-8829]Saito M, Kamonprasertsuk S, Suzuki S, Nanatani K, Oikawa H, Kushiro K, Takai M, Chen P.-T, Chen E.H.-L, Chen R.P.-Y, Takahashi S.
10.1021/acs.jpcb.6b05481
4.Where the complex things are: Single molecule and ensemble spectroscopic investigations of protein folding dynamics.[Current Opinion in Structural Biology,36,(2016),1-9]Takahashi S, Kamagata K, Oikawa H.
10.1016/j.sbi.2015.11.006
[2015]
5.Complexity of the Folding Transition of the B Domain of Protein A Revealed by the High-Speed Tracking of Single-Molecule Fluorescence Time Series.[The Journal of Physical Chemistry B,119(20),(2015),6081-6091]Hiroyuki Oikawa, Kiyoto Kamagata, Munehito Arai, Satoshi Takahashi
6.Complexity of the folding transition of the b domain of protein a revealed by the high-speed tracking of single-molecule fluorescence time series.[Journal of Physical Chemistry B,119(20),(2015),6081-6091]Oikawa H, Kamagata K, Arai M, Takahashi S.
10.1021/acs.jpcb.5b00414
[2014]
7.マイクロ秒分解一分子蛍光測定で観るタンパク質の構造変化.[生物物理,54(5),(2014),276-279]小井川 浩之, 齊藤 雅嵩, 高橋 聡
10.2142/biophys.54.276
[2013]
8.ライン共焦点顕微鏡を用いた高速一分子蛍光観察.[分光研究 = Journal of the spectroscopical research of Japan,62(5),(2013),232-234]小井川 浩之, 高橋 聡
9.Microsecond dynamics of an unfolded protein by a line confocal tracking of single molecule fluorescence.[Scientific Reports,3,(2013)]Hiroyuki Oikawa, Yuta Suzuki, Masataka Saito, Kiyoto Kamagata, Munehito Arai, Satoshi Takahashi
10.Microsecond dynamics of an unfolded protein by a line confocal tracking of single molecule fluorescence..[Scientific reports,3,(2013),2151-]Oikawa H, Suzuki Y, Saito M, Kamagata K, Arai M, Takahashi S
10.1038/srep02151
http://www.ncbi.nlm.nih.gov/pubmed/23827883 http://gateway.isiknowledge.com/gateway/Gateway.cgi?&GWVersion=2&SrcAuth=TohokuUniv&SrcApp=TohokuUniv&DestLinkType=FullRecord&KeyUT=WOS:000321322100002&DestApp=WOS
[2011]
11.一分子蛍光観察法を用いたタンパク質フォールディングの解明.[高分子,60(11),(2011),801-803]小井川 浩之, 鎌形 清人, 高橋 聡
12.単一分子分光法―高分子試料のナノ世界をかいま見る新手法―タンパク質の構造変化と単一分子分光.[高分子,60(2),(2011),80-81]小井川浩之, 南後守, 藤芳暁, 松下道雄, 出羽毅久
13.Single-protein study of photoresistance of pigment-protein complex in lipid bilayer.[Chemical Physics Letters,511(1-3),(2011),135-137]Uchiyama D, Hoshino H, Otomo K, Kato T, Onda K.-I, Watanabe A, Oikawa H, Fujiyoshi S, Matsushita M, Nango M, Watanabe N, Sumino A, Dewa T.
10.1016/j.cplett.2011.06.019
http://gateway.isiknowledge.com/gateway/Gateway.cgi?&GWVersion=2&SrcAuth=TohokuUniv&SrcApp=TohokuUniv&DestLinkType=FullRecord&KeyUT=WOS:000292687900027&DestApp=WOS
14.Reconstitution of bacterial photosynthetic unit in a lipid bilayer studied by single-molecule spectroscopy at 5 K.[Physical Chemistry Chemical Physics,13(24),(2011),11615-11619]Uchiyama D, Oikawa H, Otomo K, Nango M, Dewa T, Fujiyoshia S, Matsushita M.
10.1039/c1cp20172g
http://gateway.isiknowledge.com/gateway/Gateway.cgi?&GWVersion=2&SrcAuth=TohokuUniv&SrcApp=TohokuUniv&DestLinkType=FullRecord&KeyUT=WOS:000291395200020&DestApp=WOS
[2008]
15.How deep is the potential well confining a protein in a specific conformation? A single-molecule study on temperature dependence of conformational change between 5 and 18 K.[Journal of the American Chemical Society,130(14),(2008),4580-4581]Oikawa H, Fujiyoshi S, Dewa T, Nango M, Matsushita M.
10.1021/ja078020p
http://gateway.isiknowledge.com/gateway/Gateway.cgi?&GWVersion=2&SrcAuth=TohokuUniv&SrcApp=TohokuUniv&DestLinkType=FullRecord&KeyUT=WOS:000254643900004&DestApp=WOS
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