Performance information

• A simulation study on Raman cross sections of OH and OD stretches in isotopically pure and diluted liquid water
  Tetsuyuki Takayama; Takuhiro Otosu; Shoichi Yamaguchi
  The Journal of Chemical Physics, Volume：162, Number：24, First page：244502, Jun. 2025, [Reviewed]
  The Raman scattering activity spectra of isotopically pure and diluted liquid water are theoretically calculated to examine the mole-fraction dependence of the OH- and OD-stretch cross sections. This mole-fraction dependence was once claimed to be anomalous and attributed to nuclear quantum correlations of protons and deuterons when it was discovered experimentally. The present study demonstrates that the experimental data of the mole-fraction dependence of the cross sections, as well as the Raman scattering activity spectra in the stretch region, are well reproduced by the theoretical calculations according to the quantum/classical mixed approach in which the nuclear quantum correlations are not taken into account. This suggests that the anomalous dependence does not serve as evidence of the nuclear quantum correlations. The present study provides a more plausible interpretation that the OH- and OD-stretch cross sections depend on the mole fraction because of the inter- and intra-molecular vibrational couplings.
  AIP Publishing, English, Scientific journal
  DOI：https://doi.org/10.1063/5.0276271
  DOI ID：10.1063/5.0276271, ISSN：0021-9606, eISSN：1089-7690
• A macroscopically homogeneous lipid phase exhibits leaflet-specific lipid diffusion in a glass-supported lipid bilayer
  Takuhiro Otosu; Miyuki Sakaguchi; Shoichi Yamaguchi
  Physical Chemistry Chemical Physics, Volume：27, Number：9, First page：4944, Last page：4949, Feb. 2025, [Reviewed], [Lead, Corresponding]
  Leaflet-specific lipid diffusion analysis revealed that the strength of interleaflet coupling is sensitive to the lipid composition even in the region where macroscopically homogeneous phase is observed.
  Royal Society of Chemistry (RSC), Scientific journal
  DOI：https://doi.org/10.1039/d5cp00203f
  DOI ID：10.1039/d5cp00203f, ISSN：1463-9076, eISSN：1463-9084
• A new rigid non-polarizable model for semi-heavy water: TIP4P/2005-SHW
  Tetsuyuki Takayama; Takuhiro Otosu; Shoichi Yamaguchi
  The Journal of Chemical Physics, Volume：161, Number：23, Dec. 2024, [Reviewed]
  In molecular dynamics (MD) simulations of water, rigid non-polarizable models are still valuable and widely used because of their low computational cost and excellent performance. Most of such models have been for light water (H2O) for a long time, and a few have recently been reported for heavy water (D2O). The specific models of D2O are needed because of its notably slower dynamics and stronger hydrogen bond than H2O. To our knowledge, no models of semi-heavy water (HOD) were made, although HOD is the most abundant and, therefore, most important chemical species in isotopically diluted water (IDW) prepared by mixing equal amounts of H2O and D2O. For precise MD simulations of IDW, a specific model of HOD is definitely needed. Here, we report the development of a new rigid non-polarizable model of HOD, TIP4P/2005-SHW, on the basis of the most popular H2O model, TIP4P/2005, and its D2O counterpart, TIP4P/2005-HW. We show the details of the development and demonstrate the high reproducibility of TIP4P/2005-SHW in terms of the density, the temperature of maximum density, the viscosity, and the diffusion coefficient.
  AIP Publishing, Scientific journal
  DOI：https://doi.org/10.1063/5.0240271
  DOI ID：10.1063/5.0240271, ISSN：0021-9606, eISSN：1089-7690
• Diffusion of Multiple Species Resolved by Fluorescence Lifetime Recovery after Photobleaching (FLRAP)
  Ikumi Mori; Shun Terasaka; Shoichi Yamaguchi; Takuhiro Otosu
  Analytical Chemistry, Volume：96, Number：12, First page：4854, Last page：4859, Mar. 2024, [Reviewed], [Last, Corresponding]
  American Chemical Society (ACS), Scientific journal
  DOI：https://doi.org/10.1021/acs.analchem.3c05181
  DOI ID：10.1021/acs.analchem.3c05181, ISSN：0003-2700, eISSN：1520-6882
• Theoretical and experimental OD-stretch vibrational spectroscopy of heavy water
  Tetsuyuki Takayama; Takuhiro Otosu; Shoichi Yamaguchi
  The Journal of Chemical Physics, Volume：160, Number：10, Mar. 2024, [Reviewed]
  In view of the current situation in which the OD-stretch vibrational spectra have been scarcely computed with non-polarizable rigid D2O models, we investigate the IR and Raman spectra of D2O by using a newly-reported model TIP4P/2005-HW. From the comparison between the calculations and experimental data, we find the excellent performance of TIP4P/2005-HW for vibrational spectroscopy of D2O in the same manner as TIP4P/2005 for H2O, although one may still conveniently employ an alternative method that regards OH as putative OD to calculate the OD-stretch spectra with similar quality from TIP4P/2005 trajectories. We also demonstrate that the appropriate setting for the spectral simulation of D2O under the time-averaging approximation reflects the slower dynamics (i.e., slower motion of translation and rotation due to the heavier mass and stronger hydrogen bond) of D2O than H2O. Moreover, we show from the theoretical calculations that the established interpretation of the OH-stretch spectra of H2O is finely applicable to the OD-stretch of D2O.
  AIP Publishing, Scientific journal
  DOI：https://doi.org/10.1063/5.0200623
  DOI ID：10.1063/5.0200623, ISSN：0021-9606, eISSN：1089-7690
• Peripheral adsorption of polylysine on one leaflet of a lipid bilayer reduces the lipid diffusion of both leaflets
  Kosei Shimizu; Miyuki Sakaguchi; Shoichi Yamaguchi; Takuhiro Otosu
  Physical Chemistry Chemical Physics, Volume：26, Number：11, First page：8873, Last page：8878, Feb. 2024, [Reviewed], [Last, Corresponding]
  Leaflet-specific lipid diffusion analysis revealed that polylysine adsorption on one leaflet of a lipid bilayer is sensed by the opposite leaflet.
  Royal Society of Chemistry (RSC), Scientific journal
  DOI：https://doi.org/10.1039/d3cp04882a
  DOI ID：10.1039/d3cp04882a, ISSN：1463-9076, eISSN：1463-9084
• Appraisal of TIP4P-type models at water surface
  Shoichi Yamaguchi; Tetsuyuki Takayama; Takuhiro Otosu
  The Journal of Chemical Physics, Volume：159, Number：17, Nov. 2023, [Reviewed]
  In view of the current situation in which non-polarizable rigid water models have been scarcely examined against surface-specific properties, we appraise TIP4P-type models at the liquid water surface on the basis of heterodyne-detected sum frequency generation (HD-SFG) spectroscopy. We find in the HD-SFG spectrum of the water surface that the peak frequency of the hydrogen-bonded OH band, the half width at half maximum of the hydrogen-bonded OH band, and the full width at half maximum of the free OH band are best reproduced by TIP4P, TIP4P/Ew, and TIP4P/Ice, respectively, whereas it is already well known that TIP4P/2005 best reproduces the surface tension. These TIP4P-type models perform better at the water surface in terms of the present appraisal items than some polarizable models in the literature.
  AIP Publishing, Scientific journal
  DOI：https://doi.org/10.1063/5.0171999
  DOI ID：10.1063/5.0171999, ISSN：0021-9606, eISSN：1089-7690
• Transferability of vibrational spectroscopic map from TIP4P to TIP4P-like water models
  Tetsuyuki Takayama; Takuhiro Otosu; Shoichi Yamaguchi
  The Journal of Chemical Physics, Volume：158, Number：13, Apr. 2023, [Reviewed]
  We computed the IR, Raman, and sum frequency generation spectra of water in the OH-stretch region by employing the quantum/classical mixed approach that consists of a vibrational spectroscopic map and molecular dynamics (MD) simulation. We carried out the MD simulation with the TIP4P, TIP4P/2005, and TIP4P/Ice models and applied the map designed for TIP4P by Skinner et al. to each MD trajectory. Although the map is not tuned for TIP4P-like models, TIP4P/2005 and TIP4P/Ice provide the best reproduction of the experimental vibrational spectra of liquid water and crystalline ice, respectively. This result demonstrates the transferability of the map from TIP4P to TIP4P/2005 and TIP4P/Ice, meaning that one can choose an appropriate TIP4P-like model to calculate the vibrational spectra of an aqueous system without rebuilding the map.
  AIP Publishing, Scientific journal
  DOI：https://doi.org/10.1063/5.0146084
  DOI ID：10.1063/5.0146084, ISSN：0021-9606, eISSN：1089-7690
• Experimental and Theoretical Heterodyne-Detected Sum Frequency Generation Spectroscopy of Isotopically Pure and Diluted Water Surfaces　　　　　　　　　　　　　　　
  Shoichi Yamaguchi; Tetsuyuki Takayama; Yuki Goto; Takuhiro Otosu; Takuma Yagasaki
  The Journal of Physical Chemistry Letters, Oct. 2022, [Reviewed]
  Scientific journal
  DOI：https://doi.org/10.1021/acs.jpclett.2c02533
  DOI ID：10.1021/acs.jpclett.2c02533, ORCID：120487669
• Experimental and Theoretical Raman Spectroscopy of Isotopically Pure and Diluted Ice VI　　　　　　　　　　　　　　　
  Tetsuyuki Takayama; Kota Kishi; Takuhiro Otosu; Takuma Yagasaki; Shoichi Yamaguchi
  The Journal of Physical Chemistry C, Oct. 2022, [Reviewed]
  Scientific journal
  DOI：https://doi.org/10.1021/acs.jpcc.2c05133
  DOI ID：10.1021/acs.jpcc.2c05133, ORCID：120088265
• Raman spectroscopy of isotopically pure and diluted high‐ and low‐density amorphous ices
  Senri Ishihara; Tetsuyuki Takayama; Miyuki Sakaguchi; Takuhiro Otosu; Takuma Yagasaki; Yoshiharu Suzuki; Shoichi Yamaguchi
  Journal of Raman Spectroscopy, Feb. 2022, [Reviewed]
  Wiley, Scientific journal
  DOI：https://doi.org/10.1002/jrs.6322
  DOI ID：10.1002/jrs.6322, ISSN：0377-0486, eISSN：1097-4555
• Progress in phase-sensitive sum frequency generation spectroscopy
  Shoichi Yamaguchi; Takuhiro Otosu
  Physical Chemistry Chemical Physics, Volume：23, Number：34, First page：18253, Last page：18267, Jun. 2021, [Reviewed]
  Representative methods of surface-selective phase-sensitive sum frequency generation spectroscopy are reviewed in terms of interferometer implementation for optical heterodyne detection.
  Royal Society of Chemistry (RSC), Scientific journal
  DOI：https://doi.org/10.1039/d1cp01994e
  DOI ID：10.1039/d1cp01994e, ISSN：1463-9076, eISSN：1463-9084
• Leaflet-specific Lipid Diffusion Revealed by Fluorescence Lifetime Correlation Analyses　　　　　　　　　　　　　　　
  Takuhiro Otosu; Shoichi Yamaguchi
  CHEMISTRY LETTERS, Volume：49, Number：12, First page：1473, Last page：1480, Dec. 2020, [Reviewed], [Invited], [Lead]
  English
  DOI：https://doi.org/10.1246/cl.200539
  DOI ID：10.1246/cl.200539, ISSN：0366-7022, eISSN：1348-0715, Web of Science ID：WOS:000598377200011
• Effect of electrostatic interaction on the leaflet-specific diffusion in a supported lipid bilayer revealed by fluorescence lifetime correlation analysis　　　　　　　　　　　　　　　
  Takuhiro Otosu; Shoichi Yamaguchi
  PHYSICAL CHEMISTRY CHEMICAL PHYSICS, Volume：22, Number：3, First page：1242, Last page：1249, Jan. 2020, [Reviewed], [Lead]
  English, Scientific journal
  DOI：https://doi.org/10.1039/c9cp05833h
  DOI ID：10.1039/c9cp05833h, ISSN：1463-9076, eISSN：1463-9084, Web of Science ID：WOS:000509371400030
• Multifocus Fluorescence Correlation Spectroscopy with Spatially Separated Excitation Beams　　　　　　　　　　　　　　　
  Takuhiro Otosu; Kunihiko Ishii; Tahei Tahara
  BULLETIN OF THE CHEMICAL SOCIETY OF JAPAN, Volume：92, Number：9, First page：1495, Last page：1502, Sep. 2019, [Reviewed], [Lead]
  English, Scientific journal
  DOI：https://doi.org/10.1246/bcsj.20190109
  DOI ID：10.1246/bcsj.20190109, ISSN：0009-2673, eISSN：1348-0634, Web of Science ID：WOS:000482728000012
• Reduction of glass-surface charge density slows the lipid diffusion in the proximal leaflet of a supported lipid bilayer　　　　　　　　　　　　　　　
  Takuhiro Otosu; Shoichi Yamaguchi
  JOURNAL OF CHEMICAL PHYSICS, Volume：151, Number：2, Jul. 2019, [Reviewed], [Lead]
  English, Scientific journal
  DOI：https://doi.org/10.1063/1.5103221
  DOI ID：10.1063/1.5103221, ISSN：0021-9606, eISSN：1089-7690, Web of Science ID：WOS:000486055700034
• Perspective on sum frequency generation spectroscopy of ice surfaces and interfaces　　　　　　　　　　　　　　　
  Shoichi Yamaguchi; Yudai Suzuki; Yuki Nojima; Takuhiro Otosu
  CHEMICAL PHYSICS, Volume：522, First page：199, Last page：210, Jun. 2019, [Reviewed]
  English, Scientific journal
  DOI：https://doi.org/10.1016/j.chemphys.2019.03.005
  DOI ID：10.1016/j.chemphys.2019.03.005, ISSN：0301-0104, eISSN：1873-4421, Web of Science ID：WOS:000466713000027
• Quantifying the Diffusion of Lipids in the Proximal/Distal Leaflets of a Supported Lipid Bilayer by Two-Dimensional Fluorescence Lifetime Correlation Spectroscopy　　　　　　　　　　　　　　　
  Takuhiro Otosu; Shoichi Yamaguchi
  JOURNAL OF PHYSICAL CHEMISTRY B, Volume：122, Number：45, First page：10315, Last page：10319, Nov. 2018, [Reviewed], [Lead]
  English, Scientific journal
  DOI：https://doi.org/10.1021/acs.jpcb.8b08614
  DOI ID：10.1021/acs.jpcb.8b08614, ISSN：1520-6106, Web of Science ID：WOS:000451101100006
• Two-Dimensional Fluorescence Lifetime Correlation Spectroscopy: Concepts and Applications　　　　　　　　　　　　　　　
  Takuhiro Otosu; Shoichi Yamaguchi
  MOLECULES, Volume：23, Number：11, Nov. 2018, [Reviewed], [Lead]
  English
  DOI：https://doi.org/10.3390/molecules23112972
  DOI ID：10.3390/molecules23112972, eISSN：1420-3049, Web of Science ID：WOS:000451641900244
• Total Internal Reflection Two-Dimensional Fluorescence Lifetime Correlation Spectroscopy　　　　　　　　　　　　　　　
  Takuhiro Otosu; Shoichi Yamaguchi
  JOURNAL OF PHYSICAL CHEMISTRY B, Volume：122, Number：22, First page：5758, Last page：5764, Jun. 2018, [Reviewed]
  English, Scientific journal
  DOI：https://doi.org/10.1021/acs.jpcb.8b01176
  DOI ID：10.1021/acs.jpcb.8b01176, ISSN：1520-6106, SCOPUS ID：85048247541, Web of Science ID：WOS:000435019600004
• Local pH at the surface of hen egg white lysozyme　　　　　　　　　　　　　　　
  Takuhiro Otosu; Kaito Kobayashi; Shoichi Yamaguchi
  CHEMICAL PHYSICS LETTERS, Volume：693, First page：165, Last page：169, Feb. 2018, [Reviewed]
  English, Scientific journal
  DOI：https://doi.org/10.1016/j.cplett.2018.01.026
  DOI ID：10.1016/j.cplett.2018.01.026, ISSN：0009-2614, eISSN：1873-4448, SCOPUS ID：85040701289, Web of Science ID：WOS:000424631900026
• Communication: Development of standing evanescent-wave fluorescence correlation spectroscopy and its application to the lateral diffusion of lipids in a supported lipid bilayer　　　　　　　　　　　　　　　
  Takuhiro Otosu; Shoichi Yamaguchi
  JOURNAL OF CHEMICAL PHYSICS, Volume：147, Number：4, First page：041101, Jul. 2017, [Reviewed], [Lead]
  English, Scientific journal
  DOI：https://doi.org/10.1063/1.4985871
  DOI ID：10.1063/1.4985871, ISSN：0021-9606, eISSN：1089-7690, Web of Science ID：WOS:000406347200002
• Highly Heterogeneous Nature of the Native and Unfolded States of the B Domain of Protein A Revealed by Two-Dimensional Fluorescence Lifetime Correlation Spectroscopy　　　　　　　　　　　　　　　
  Takuhiro Otosu; Kunihiko Ishii; Hiroyuki Oikawa; Munehito Arai; Satoshi Takahashi; Tahei Tahara
  JOURNAL OF PHYSICAL CHEMISTRY B, Volume：121, Number：22, First page：5463, Last page：5473, Jun. 2017, [Reviewed]
  English, Scientific journal
  DOI：https://doi.org/10.1021/acs.jpcb.7b00546
  DOI ID：10.1021/acs.jpcb.7b00546, ISSN：1520-6106, Web of Science ID：WOS:000403191700001
• Standing evanescent-wave fluorescence correlation spectroscopy for analyzing the translational diffusion in bio-membranes　　　　　　　　　　　　　　　
  Takuhiro Otosu; Shoichi Yamaguchi
  ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, Volume：252, Aug. 2016, [Reviewed], [Lead]
  English
  ISSN：0065-7727, Web of Science ID：WOS:000431460201108
• Microsecond protein dynamics observed at the single-molecule level　　　　　　　　　　　　　　　
  Takuhiro Otosu; Kunihiko Ishii; Tahei Tahara
  NATURE COMMUNICATIONS, Volume：6, Jul. 2015, [Reviewed], [Lead]
  English, Scientific journal
  DOI：https://doi.org/10.1038/ncomms8685
  DOI ID：10.1038/ncomms8685, ISSN：2041-1723, Web of Science ID：WOS:000358858100029
• Two-Dimensional Fluorescence Lifetime Correlation Spectroscopy on the Folding Mechanism of B Domain of Protein A　　　　　　　　　　　　　　　
  Takuhiro Otosu; Kunihiko Ishii; Hiroyuki Oikawa; Munehito Arai; Satoshi Takahashi; Tahei Tahara
  BIOPHYSICAL JOURNAL, Volume：108, Number：2, First page：501A, Last page：501A, Jan. 2015, [Reviewed]
  English
  DOI：https://doi.org/10.1016/j.bpj.2014.11.2747
  DOI ID：10.1016/j.bpj.2014.11.2747, ISSN：0006-3495, eISSN：1542-0086, Web of Science ID：WOS:000362849600141
• 1P055 Study of BdpA folding by two-dimensional fluorescence lifetime correlation spectroscopy : Comprehensive analysis of two BdpA mutants(01C. Protein : Property,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))　　　　　　　　　　　　　　　
  Otosu Takuhiro; Ishii Kunihiko; Oikawa Hiroyuki; Arai Munehito; Takahashi Satoshi; Tahara Tahei
  Seibutsu Butsuri, Volume：54, Number：1, First page：S150, 2014
  The Biophysical Society of Japan General Incorporated Association, English
  DOI：https://doi.org/10.2142/biophys.54.S150_1
  DOI ID：10.2142/biophys.54.S150_1, CiNii Articles ID：110009932279
• Microsecond Conformational Dynamics of Cytochrome C Revealed by Two-Dimentional Fluorescence Lifetime Correlation Spectroscopy　　　　　　　　　　　　　　　
  Takuhiro Otosu; Kunihiko Ishii; Tahei Tahara
  BIOPHYSICAL JOURNAL, Volume：106, Number：2, First page：459A, Last page：459A, Jan. 2014, [Reviewed]
  English
  DOI：https://doi.org/10.1016/j.bpj.2013.11.2603
  DOI ID：10.1016/j.bpj.2013.11.2603, ISSN：0006-3495, eISSN：1542-0086, Web of Science ID：WOS:000337000402557
• Note: Simple calibration of the counting-rate dependence of the timing shift of single photon avalanche diodes by photon interval analysis　　　　　　　　　　　　　　　
  Takuhiro Otosu; Kunihiko Ishii; Tahei Tahara
  REVIEW OF SCIENTIFIC INSTRUMENTS, Volume：84, Number：3, Mar. 2013, [Reviewed]
  English, Scientific journal
  DOI：https://doi.org/10.1063/1.4794769
  DOI ID：10.1063/1.4794769, ISSN：0034-6748, eISSN：1089-7623, Web of Science ID：WOS:000316966200057
• 3P052 Two-dimensional fluorescence lifetime correlation spectroscopy on the conformational dynamics of the unfolded state of BdpA(01A. Protein: Structure,Poster)　　　　　　　　　　　　　　　
  Otosu Takuhiro; Ishii Kunihiko; Oikawa Hiroyuki; Arai Munehito; Takahashi Satoshi; Tahara Tahei
  Seibutsu Butsuri, Volume：53, Number：1, First page：S220, 2013
  The Biophysical Society of Japan General Incorporated Association, English
  DOI：https://doi.org/10.2142/biophys.53.S220_4
  DOI ID：10.2142/biophys.53.S220_4, CiNii Articles ID：110009819856
• Multiple conformational state of human serum albumin around single tryptophan residue at various pH revealed by time-resolved fluorescence spectroscopy　　　　　　　　　　　　　　　
  Takuhiro Otosu; Etsuko Nishimoto; Shoji Yamashita
  JOURNAL OF BIOCHEMISTRY, Volume：147, Number：2, First page：191, Last page：200, Feb. 2010, [Reviewed], [Lead]
  English, Scientific journal
  DOI：https://doi.org/10.1093/jb/mvp175
  DOI ID：10.1093/jb/mvp175, ISSN：0021-924X, Web of Science ID：WOS:000274344400006
• Fluorescence Decay Characteristics of Indole Compounds Revealed by Time-Resolved Area-Normalized Emission Spectroscopy　　　　　　　　　　　　　　　
  Takuhiro Otosu; Etsuko Nishimoto; Shoji Yamashita
  JOURNAL OF PHYSICAL CHEMISTRY A, Volume：113, Number：12, First page：2847, Last page：2853, Mar. 2009, [Reviewed]
  English, Scientific journal
  DOI：https://doi.org/10.1021/jp8078937
  DOI ID：10.1021/jp8078937, ISSN：1089-5639, Web of Science ID：WOS:000264348800024
• The unfolding of alpha-momorcharin proceeds through the compact folded intermediate　　　　　　　　　　　　　　　
  Yukihiro Fukunaga; Etsuko Nishimoto; Takuhiro Otosu; Yasutaka Murakami; Shoji Yamashita
  JOURNAL OF BIOCHEMISTRY, Volume：144, Number：4, First page：457, Last page：466, Oct. 2008, [Reviewed]
  English, Scientific journal
  DOI：https://doi.org/10.1093/jb/mvn088
  DOI ID：10.1093/jb/mvn088, ISSN：0021-924X, Web of Science ID：WOS:000259770200006
• Heterogeneous packing in the folding/unfolding intermediate state of bitter gourd trypsin inhibitor　　　　　　　　　　　　　　　
  Daisuke Takahashi; Shuzo Matsumoto; Etsuko Nishimoto; Takuhiro Otosu; Shoji Yamashita
  BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, Volume：72, Number：6, First page：1498, Last page：1505, Jun. 2008, [Reviewed]
  English, Scientific journal
  DOI：https://doi.org/10.1271/bbb.80009
  DOI ID：10.1271/bbb.80009, ISSN：0916-8451, eISSN：1347-6947, Web of Science ID：WOS:000257305300012
• 2P-091 The fluorescence spectroscopic characterization of the protein folding/unfolding intermediate state in the acidic condition(The 46th Annual Meeting of the Biophysical Society of Japan)　　　　　　　　　　　　　　　
  Otosu Takuhiro; Nishimoto Etsuko; Murakami Yasutaka; Yamashita Shoji
  Seibutsu Butsuri, Volume：48, First page：S89, 2008
  The Biophysical Society of Japan General Incorporated Association, English
  DOI：https://doi.org/10.2142/biophys.48.S89_2
  DOI ID：10.2142/biophys.48.S89_2, CiNii Articles ID：110007013592
• 2P-087 The conformation and dynamics of the refolded momorcharins(The 46th Annual Meeting of the Biophysical Society of Japan)　　　　　　　　　　　　　　　
  Murakami Yasutaka; Nishimoto Etsuko; Otosu Takuhiro; Yamashita Shoji
  Seibutsu Butsuri, Volume：48, First page：S88, 2008
  The Biophysical Society of Japan General Incorporated Association, English
  DOI：https://doi.org/10.2142/biophys.48.S88_5
  DOI ID：10.2142/biophys.48.S88_5, CiNii Articles ID：110007013588
• Spectrally and time-resolved fluorescence spectroscopic study on melittin-calmodulin interaction　　　　　　　　　　　　　　　
  Takuhiro Otosu; Etsuko Nishimoto; Shoji Yamashita
  JOURNAL OF BIOCHEMISTRY, Volume：142, Number：5, First page：655, Last page：661, Nov. 2007, [Reviewed]
  English, Scientific journal
  DOI：https://doi.org/10.1093/jb/mvm180
  DOI ID：10.1093/jb/mvm180, ISSN：0021-924X, Web of Science ID：WOS:000253630200014
• 2P046 Time-resolved fluorescence study on multiple dielectric relaxation properties of single tryptophan residue in RNase T1(Proteins-structure and structure-function relationship,Oral Presentations)　　　　　　　　　　　　　　　
  Otosu Takuhiro; Nishimoto Etsuko; Miyazaki Yoshifumi; Yamashita Shoji
  Seibutsu Butsuri, Volume：47, First page：S124, 2007
  The Biophysical Society of Japan General Incorporated Association, English
  DOI：https://doi.org/10.2142/biophys.47.S124_3
  DOI ID：10.2142/biophys.47.S124_3, CiNii Articles ID：110006562022
• The partially unfolded state of beta-momorcharin characterized with steady-state and time-resolved fluorescence studies　　　　　　　　　　　　　　　
  Yukihiro Fukunaga; Etsuko Nishimoto; Katsumi Yamashita; Takuhiro Otosu; Shoji Yamashita
  JOURNAL OF BIOCHEMISTRY, Volume：141, Number：1, First page：9, Last page：18, Jan. 2007, [Reviewed]
  English, Scientific journal
  DOI：https://doi.org/10.1093/jb/mvm002
  DOI ID：10.1093/jb/mvm002, ISSN：0021-924X, Web of Science ID：WOS:000244866600002
• 2P010 Fluorescence spectroscopic study on the CaM-target protein interaction-Interaction with melittin(29. Protein structure and dynamics (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)　　　　　　　　　　　　　　　
  Otosu Takuhiro; Nishimoto Etsuko; Fukunaga Yukihiro; Miyazaki Yoshifumi; Yamashita Shoji
  Seibutsu Butsuri, Volume：46, Number：2, First page：S298, 2006
  The Biophysical Society of Japan General Incorporated Association, English
  DOI：https://doi.org/10.2142/biophys.46.S298_2
  DOI ID：10.2142/biophys.46.S298_2, CiNii Articles ID：110006193971
• 1P051 Protein-protein interaction between calmodulin and glutamic acid decarboxylase　　　　　　　　　　　　　　　
  Otosu T.; Matsumoto T.; Nishimoto E.; Yamashita S.; Yamaura I.
  Seibutsu Butsuri, Volume：45, First page：S44, 2005
  The Biophysical Society of Japan General Incorporated Association, Japanese
  DOI：https://doi.org/10.2142/biophys.45.S44_3
  DOI ID：10.2142/biophys.45.S44_3, CiNii Articles ID：110004571032

• Advanced Photon Counting: Applications, Methods, Instrumentation　　　　　　　　　　　　　　　
  Ishii Kunihiko; Otosu Takuhiro; Tahara Tahei, [Contributor], Chapter 9 Lifetime-weighted FCS and 2D FLCS: Advanced application of time-tagged TCSPC
  Springer, 2015
  English
  ISBN：9783319156361

• 新規分光計測による混合脂質二重膜の新たな相境界の探索　　　　　　　　　　　　　　　
  Apr. 2023 - Mar. 2026
  Grant amount(Total)：4550000, Direct funding：3500000, Indirect funding：1050000
  Grant number：23K04662
• アミロイド形成を促す脂質‐蛋白質間相互作用の分子機構解明　　　　　　　　　　　　　　　
  01 Apr. 2019 - 31 Mar. 2023
  Grant amount(Total)：15600000, Direct funding：12000000, Indirect funding：3600000
  Grant number：19H02669
• 膜融合の分子機構解明に向けた脂質二重膜間相互作用の分光学的研究　　　　　　　　　　　　　　　
  Sep. 2020 - Aug. 2022
  Principal investigator
• Development and application of novel flow velocimetry at the solid-liquid interface　　　　　　　　　　　　　　　
  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research, Grant-in-Aid for Challenging Research (Exploratory), 30 Jun. 2017 - 31 Mar. 2019
  Otosu Takuhiro, Saitama University
  Grant amount(Total)：6110000, Direct funding：4700000, Indirect funding：1410000
  Understanding the flow of particles at the solid-liquid interface has important implications on the regulation of the effective chemical reaction at the interface as well as the elucidation of blood flow at the inner surface of blood vessel. In the present study, I aimed at developing new optical technique for flow velocity measurement at the solid-liquid interface.
  For that purpose, I applied a novel fluorescence microscope system that I recently developed for biomembrane study. This system utilizes the interference of evanescent waves to excite samples. The fringe pattern (standing evanescent-wave) generated by the interference of the evanescent waves enables us to analyze the flow velocity with high spatial resolution beyond the diffraction limit. To apply this new technique to the flow-velocity measurement, I constructed surface-sensitive flow velocimetry by combining standing evanescent-wave fluorescence microscope with microfluidic device.
  Grant number：17K19097
• Protein-ligand complex formation revealed by fluorescence lifetime-correlation analysis　　　　　　　　　　　　　　　
  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research, Grant-in-Aid for Young Scientists (B), 01 Apr. 2015 - 31 Mar. 2017
  OTOSU Takuhiro, Saitama University
  Grant amount(Total)：4160000, Direct funding：3200000, Indirect funding：960000
  Conformational fluctuations of proteins are highly relevant to their biological functions. To this aim, we developed two-dimensional fluorescence lifetime correlation spectroscopy (2D FLCS) which analyze the conformational dynamics of biomolecules in an equilibrium by the correlation analysis of fluorescence lifetime. The aim of this study is to extend 2D FLCS to analyze the conformational dynamics in a non-equilibrium condition. For this purpose, I developed new 2D FLCS instrument which utilizes two laser pulses (UV pulse and visible pulse). UV pulse is used for uncaging the caged compound to transiently increase the ligand concentration in the focal region. The conformational change of protein caused by the interaction with the ligand is then monitored through visible pulse. Preliminary results clearly showed that the instrument developed here is applicable to analyze the ligand-induced conformational changes of proteins with 2D FLCS.
  Grant number：15K17814