Language：English   Publishing type：Research paper (scientific journal)  

Evolution should have played important roles in determining folding mechanisms and structures of proteins. In this article we discuss how the folding mechanisms had been affected by the early stage of evolution through which the uniqueness of structure had developed. Although the process of such early-time evolution has remained a mystery, a plausible scenario is that the evolution of proteins toward the ordered structures was guided by functional selection pressure as demonstrated in vitro and in silico. We examine the in silico functional selection of sequences and show that there is a significant correlation between two different processes toward the unique 3D structure, the evolutionary development of structure through sequence selection, and the folding process of the resultant sequence. This finding could be rephrased as protein folding recapitulates the emergence of topology in the molecular evolution. The correlation suggests a guideline for engineering foldable proteins.

DOI： 10.1073/pnas.0509163102

Authorship：Lead author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

Actin-myosin (actomyosin) generates mechanical force by consuming ATP molecules. We apply the energy landscape perspective to address a controversial issue as to whether the myosin head moves with multiple steps after a single ATP hydrolysis or only a single mechanical event of the lever-arm swinging follows a single ATP hydrolysis. Here we propose a theoretical model in which the refolding of the partially unfolded actomyosin complex and the movement of the myosin head along the actin filament are coupled. A single ATP hydrolysis is followed by the formation of a high free-energy partially unfolded actomyosin complex, which then gradually refolds with a concomitant multiple stepping movement on the way to the lowest free-energy rigor state. The model quantitatively explains the single-molecular observation of the multiple stepping movement and is consistent with structural observations of the disorder in the actomyosin-binding process. The model also explains the observed variety in dwell time before each step, which is not accounted for by previous models, such as the lever-arm or ratchet models.

DOI： 10.1073/pnas.132711799

Authorship：Lead author   Language：English   Publishing type：Research paper (other academic)  

DOI： 10.1016/j.bpj.2019.11.2449

Web of Science

Authorship：Lead author   Language：English   Publishing type：Research paper (conference, symposium, etc.)  

DOI： 10.1007/s00249-019-01373-4

Web of Science

Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.2142/biophysico.15.0_136

Web of Science

Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.1038/s41598-017-17717-z

Authorship：Last author   Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.2142/biophysico.13.0_281

Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.2142/biophysico.13.0_149

Authorship：Last author   Language：Japanese   Publishing type：Research paper (scientific journal)  

DOI： 10.2142/biophys.56.106

Authorship：Lead author,　Last author,　Corresponding author   Language：Japanese   Publishing type：Research paper (scientific journal)  

Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.1021/acs.jcim.5b00134

Authorship：Lead author,　Last author,　Corresponding author   Language：Japanese   Publishing type：Research paper (scientific journal)  

DOI： 10.2142/biophys.55.148

Authorship：Last author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

A long-standing controversy on the mechanism of an actomyosin motor is the role of the Brownian motion of the myosin head in force generation. In order to shed light on this problem, we calculate free-energy landscapes of interaction between an actin filament and the head (S1) of myosin II by using a coarse-grained model of actomyosin. The results show that the free-energy landscape has a global gradient toward the strong-binding site on actin filament, which explains the biased Brownian motion of myosin S1 observed in a single-molecule experiment [Kitamura et al., Nature, 1999, 397, 129 and Biophysics, 2005, 1, 1]. The distinct global gradient in the landscape is brought about only when the conformation of loop 2 at the actin interface of myosin S1 is flexible. The conformational flexibility of loop 3 also contributes to the gradient in the landscape by compensating the role of loop 2. Though the structure of loop 2 is expanded in the weak-binding state, loop 2 shows the larger fluctuation of compaction and expansion due to the actin-myosin interactions as myosin S1 moves toward the strong-binding site on actin filament. Hence, the increase in the compaction-expansion fluctuation of loop 2, the stronger binding of myosin to actin, and the biased Brownian motion of myosin S1 are coupled with each other and should take place in a concurrent way. This predicted coupling should provide opportunities to further test the hypothesis of the biased Brownian motion in actomyosin.

DOI： 10.1039/C3CP54464H

Authorship：Lead author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

The mechanism of allosteric conformational transitions of Escherichia coli dihydrofolate reductase (DHFR) is investigated theoretically by applying a newly developed coarse-grained model. Functional forms of interaction potentials in the model depend on the local structural environments around those interactions to represent the many-residue effects due to atomic packing in each local region, and hence, this model is called "the chameleon model". The chameleon model consistently describes the free-energy landscape of two conformational transitions in the catalytic cycle of DHFR, which we call conformational transition 1 (CT1) and conformational transition 2 (CT2); CT1 is accompanied by the hydride transfer reaction, and CT2 is accompanied by the product ligand release. The transition state of CT1 is entropically stabilized by the disordering of loops at the peripheral regions of the protein, which enhances the positively correlated fluctuations at the center part of the protein, showing that the allosteric communication between distant regions through the central region is intrinsically associated with the entropic stabilization of the transition state. The transition state of CT2 is entropically stabilized through the mechanism that enhances the breathing motion of two domains, showing that the difference in the distribution of interactions brings about the difference in the transition mechanism between CT1 and CT2. The chameleon model opens a way to consistently describe the dynamical energy landscape of enzymatic reactions.

DOI： 10.1021/jp402071m

Language：English   Publishing type：Research paper (scientific journal)  

Eukaryotic genome is organized in a set of chromosomes each of which consists of a chain of DNA and associated proteins. Processes involving DNA such as transcription, duplication, and repair, therefore, should be intrinsically related to the three-dimensional organization of the genome. In this article, we develop a computational model of the three-dimensional organization of the haploid genome of interphase budding yeast by regarding chromosomes as chains moving under the constraints of nuclear structure and chromatin-chromatin interactions. The simulated genome structure largely fluctuates with the diffusive movement of chromosomes. This fluctuation, however, is not completely random, as parts of chromosomes distribute in characteristic ways to form "territories" in the nucleus. By suitably taking account of constraints arising from the data of the chromosome-conformation-capture measurement, the model explains the observed fluorescence data of chromosome distributions and motions.

DOI： 10.1016/j.bpj.2011.12.005

Language：English   Publishing type：Research paper (scientific journal)  

In recent experimental reports, robust circadian oscillation of the phosphorylation level of KaiC has been reconstituted by incubating three cyanobacterial proteins, KaiA, KaiB, and KaiC, with ATP in vitro. This reconstitution indicates that protein-protein interactions and the associated ATP hydrolysis suffice to generate the oscillation, and suggests that the rhythm arising from this protein-based system is the circadian clock pacemaker in cyanobacteria. The mechanism of this reconstituted oscillation, however, remains elusive. In this study, we extend our previous model of oscillation by explicitly taking two phosphorylation sites of KaiC into account and we apply the extended model to the problem of synchrony of two oscillatory samples mixed at different phases. The agreement between the simulated and observed data suggests that the combined mechanism of the allosteric transition of KaiC hexamers and the monomer shuffling between them plays a key role in synchronization among KaiC hexamers and hence underlies the population-level oscillation of the ensemble of Kai proteins. The predicted synchronization patterns in mixtures of unequal amounts of two samples provide further opportunities to experimentally check the validity of the proposed mechanism. This mechanism of synchronization should be important in vivo for the persistent oscillation when Kai proteins are synthesized at random timing in cyanobacterial cells.

DOI： 10.1016/j.bpj.2010.02.036

Language：English   Publishing type：Research paper (scientific journal)  

By incubating the mixture of three cyanobacterial proteins, KaiA, KaiB, and KaiC, with ATP in vitro, T. Kondo and his colleagues in recent work reconstituted the robust circadian rhythm of the phosphorylation level of KaiC. This finding indicates that protein-protein interactions and the associated hydrolysis of ATP suffice to generate the circadian rhythm. Several theoretical models have been proposed to explain the rhythm generated in this "protein-only" system, but the clear criterion to discern different possible mechanisms was not known. In this article, we discuss a model based on two basic assumptions: the assumption of the allosteric transition of a KaiC hexamer and the assumption of the monomer exchange between KaiC hexamers. The model shows a stable rhythmic oscillation of the phosphorylation level of KaiC, which is robust against changes in concentration of Kai proteins. We show that this robustness gives a clue to distinguish different possible mechanisms. We also discuss the robustness of oscillation against the change in the system size. Behaviors of the system with the cellular or subcellular size should shed light on the role of the protein-protein interactions in in vivo circadian oscillation.

DOI： 10.1529/biophysj.107.127555

Language：English   Publishing type：Research paper (scientific journal)  

Circadian rhythms in living organisms have long been attributed solely to a transcription-translation loop comprising a negative or positive feedback. The rhythms in cyanobacteria are known to be modulated by kaiC, kaiA and kaiB genes. It was recently shown, however, that their product proteins KaiC, KaiA and KaiB are sufficient to reconstitute the circadian rhythm in the phosphorylation level of KaiC in vitro. It has since been unclear why such an oscillatory behavior can occur in the absence of the apparent transcription-translation feedback. In the meantime, it has been reported that the monomer exchange between KaiC hexamers occurs in a phosphorylation-dependent manner, which suggests that the monomer shuffling is also involved in the circadian rhythm (H. Kageyama et al., Mol. Cell, 23, 161 (2006)). To further clarify the role of the monomer shuffling, we have performed a computational modeling of interactions among Kai proteins assuming the allosteric transition of KaiC hexamer as well as the monomer shuffling. The results show that the existence of both monomer shuffling and allosteric transition can synchronize the phosphorylation level of the KaiC hexamers, and stabilizes its oscillation.

DOI： 10.1371/journal.pone.0000408

Authorship：Last author   Language：Japanese   Publishing type：Research paper (scientific journal)  

DOI： 10.1295/kobunshi.51.448

Authorship：Last author,　Corresponding author   Language：Japanese   Publishing type：Research paper (scientific journal)  

Language：English   Publishing type：Research paper (scientific journal)  

Chaperonin-assisted protein folding proceeds through cycles of ATP binding and hydrolysis by GroEL, which undergoes a large structural change by the ATP binding or hydrolysis. One of the main concerns of GroEL is the mechanism of the productive and cooperative structural change of GroEL induced by the nucleotide. We studied the cooperative nature of GroEL by nucleotide titration using isothermal titration calorimetry and fluorescence spectroscopy. Our results indicated that the binding of ADP and ATP analogs to a single ring mutant (SR1), as well as that to GroEL, was non-cooperative. Only ATP induces an apparently cooperative conformational change in both proteins. Furthermore, the fluorescence changes of pyrene-labeled GroEL indicated that GroEL has two kinds of nucleotide binding sites. The fluorescence titration result fits well with a model in which two kinds of binding sites are both non-cooperative and independent of each other. These results suggest that the binding and hydrolysis of ATP may be necessary for the cooperative transition of GroEL.

DOI： 10.1016/S0167-4838(00)00274-0

Language：English   Publishing type：Research paper (scientific journal)  

The equilibrium and kinetics of the unfolding and refolding of authentic and recombinant human α-lactalbumin, the latter of which had an extra methionine residue at the N-terminus, were studied by circular dichroism spectroscopy, and the results were compared with the results for bovine and goat α-lactalbumins obtained in our previous studies. As observed in the bovine and goat proteins, the presence of the extra methionine residue in the recombinant protein remarkably destabilized the native state, and the destabilization was entirely ascribed to an increase in the rate of unfolding. The thermodynamic stability of the native state against the unfolded state was lower, and the thermodynamic stability of the molten globule state against the unfolded state was higher for the human protein than for the other α-lactalbumins previously studied. Thus, the population of the molten globule intermediate was higher during the equilibrium unfolding of human α-lactalbumin by guanidine hydrochloride. Unlike the molten globule states of the bovine and goat proteins, the human α-lactalbumin molten globule showed remarkably more intense circular dichroism ellipticity than the native state in the far-ultraviolet region below 225 nm. During refolding from the unfolded state, human α-lactalbumin thus exhibited overshoot kinetics, in which the alpha-helical peptide ellipticity exceeded the native value when the molten globule folding intermediate was formed in the burst phase. The subsequent folding involved reorganization of nonnative secondary structures. It should be noted that the rate constant of the major refolding phase was approximately the same among the three types of α-lactalbumin and that the rate constant of unfolding was accelerated 18-600 times in the human protein, and these results interpreted the lower thermodynamic stability of this protein.

DOI： 10.1021/bi001735j

Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)  

We characterized the thermodynamics of binding reactions of nucleotides ADP and ATPγS (a nonhydrolyzable analog of ATP) to GroEL in a temperature range of 5°C to 35°C by isothermal titration calorimetry. Analysis with a noncooperative binding model has shown that the bindings of nucleotides are driven enthalpically with binding constants of 7×103 M-1 and 4×104 M-1 for ADP and ATPγS, respectively, at 26°C and that the heat capacity change ΔCp is about 100 cal/molcharacterK for both the nucleotides. The stoichiometries of binding were about 8 and 9 molecules for ADP and ATPγS, respectively, per GroEL tetradecamer at 5°C, and both increased with temperature to reach about 14 (ADP) and 12 (ATPγS) for both nucleotides at 35°C. The absence of initial increase of binding heat as well as Hill coefficient less than 1.2, which were obtained from the fitting to the model curve by assuming positive cooperativity, showed that there was virtually no positive cooperativity in the nucleotide bindings. Incorporating a difference in affinity for the nucleotide (ADP and ATPγS) between the two rings of GroEL into the noncooperative binding model improved the goodness of fitting and the difference in the affinity increased with decreasing temperature.

DOI： 10.1016/S0167-4838(99)00049-7

Language：English   Publishing type：Research paper (scientific journal)  

The structure, stability, and unfolding-refolding kinetics of Escherichia coli-expressed recombinant goat α-lactalbumin were studied by circular dichroism spectroscopy, X-ray crystallography, and stopped-flow measurements, and the results were compared with those of the authentic protein prepared from goat milk. The electric properties of the two proteins were also studied by gel electrophoresis and ion-exchange chromatography. Although the overall structures of the authentic and recombinant proteins are the same, the extra methionine residue at the N terminus of the recombinant protein remarkably affects the native-state stability and the electric properties. The native state of the recombinant protein was 3.5 kcal/mol less stable than the authentic protein, and the recombinant protein was more negatively charged than the authentic one. The recombinant protein unfolded 5.7 times faster than the authentic one, although there were no significant differences in the refolding rates of the two proteins. The destabilization of the recombinant protein can be fully interpreted in terms of the increased unfolding rate of the protein, indicating that the N-terminal region remains unorganized in the transition state of refolding, and hence is not involved in the folding initiation site of the protein. A comparison of the X-ray structures of recombinant α-lactalbumin determined here with that of the authentic protein shows that the structural differences between the proteins are confined to the N-terminal region. Theoretical considerations for the differences in the conformational and solvation free energies between the proteins show that the destabilization of the recombinant protein is primarily due to excess conformational entropy of the N-terminal methionine residue in the unfolded state, and also due to less exposure of hydrophobic surface on unfolding. The results suggest that when the N-terminal region of a protein has a rigid structure, expression of the protein by E. coli, which adds the extra methionine residue, destabilizes the native state through a conformational entropy effect. It also shows that differences in the electrostatic interactions of the N-terminal amino group with the side-chain atoms of Thr38, Asp37, and Asp83 bring about a difference in the pKa value of the N-terminal amino group between the proteins, resulting in a greater negative net charge of the recombinant protein at neutral pH.

DOI： 10.1006/jmbi.1998.2362

Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.1103/PhysRevC.58.2366

Language：English   Publishing type：Research paper (scientific journal)  

Previous kaonic hydrogen X-ray experiments suffered from a poor signal-to-background level. This has been overcome in the present measurement through the use of a gaseous hydrogen target and the imposition of a two-charged-pion tagging requirement. In this paper a full technical description is given of the experimental methods employed.

DOI： 10.1016/S0168-9002(98)00201-0

Language：English   Publishing type：Research paper (scientific journal)  

DOI： 10.1103/PhysRevLett.78.3067

Authorship：Lead author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

Cascade calculations of hadronic hydrogen atoms are performed to obtain the x-ray yields as a function of the target density. An extension of Leon-Bethe's Stark mixing rates to m(not equal)0 states is made without the introduction of the parameter kSTK, which is necessary in the Borie-Leon model to enhance the Stark mixing rates. Although the energies of their L x rays are too low to observe, we can roughly estimate the 2p absorption width of pionic and kaonic hydrogen atoms from the measured K x-ray yields.

DOI： 10.1103/PhysRevC.55.73

Language：English   Publishing type：Research paper (scientific journal)  

In order to raise the throughput of low-energy X-ray signals appearing in a background of high-energy pulses, a new pulse-processor that measures the rise time of a trapezoidal waveform instead of the peak height has been developed. A rectangular pre-filter and a gated integrator are used to make the wave-shape at the shaper output linear. A rectangular pulse is formed by adding a differentiated step signal and its integration. The rise time of the trapezoidal waveform is inversely proportional to the height of the input step pulse. Therefore, processing time for a high-energy pulse is shorter than that for low-energy one. Consequently, the pile-up loss of the low-energy X-rays is reduced.

DOI： 10.1109/23.507160

Event date： 2023.11

Language：English   Presentation type：Poster presentation  

Country：Japan  

Event date： 2023.9

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：Tohoku University, Kawauchi Campus   Country：Japan  

Event date： 2023.7

Language：English   Presentation type：Poster presentation  

Country：Japan  

Event date： 2022.9

Language：English   Presentation type：Poster presentation  

Country：Japan  

Event date： 2022.9

Language：English   Presentation type：Poster presentation  

Country：Japan  

Event date： 2021.11

Language：English   Presentation type：Oral presentation (general)  

Venue：Online   Country：Japan  

We study the conformational transition by coarse-grained molecular dynamics simulation. We use chameleon model, an extended model of Go-like model with which we can calculate the free energy landscape of confrontational transitions (Terada et al., J. Phys. Chem. B 117, 12864 (2013)). We focus on the NtrC receiver domain which exhibits allosteric transition with the register shift of anα-helix. The chameleon model was applied to NtrC and the simulation results showed a free energy landscape with two states corresponding to active and inactive states. Therefore, we performed a free energy landscape analysis of conformational transition of NtrC. Free energy landscape analysis shows that the α-helix rotates in the intermediate state between active and inactive states.

Event date： 2021.11

Language：English   Presentation type：Oral presentation (general)  

Venue：Online   Country：Japan  

Chameleon model is the model for description of two-state conformational transition of proteins. In the model, the interaction between residues changes depending on how similar the environment around the residues is to one state and the other state. We applied the model to the conformational transition of adenylate kinase. We calculated the rates of conformational transition from the free energy difference between fully closed state and transition state which is the rate-limiting step of the enzymatic activity. We found that the temperature dependence of calculated conformational transition rates is similar to that of experimental enzymatic activity, showing that chameleon model gives a good approximation of free energy landscape of conformational transition.

Event date： 2020.9

Language：English   Presentation type：Poster presentation  

Country：Japan  

Event date： 2020.9

Language：English   Presentation type：Poster presentation  

Country：Japan  

Event date： 2020.9

Language：English   Presentation type：Poster presentation  

Country：Japan  

Event date： 2020.3

Language：Japanese   Presentation type：Poster presentation  

Venue：名古屋大学   Country：Japan  

Event date： 2020.2

Language：English   Presentation type：Poster presentation  

Country：United States  

Event date： 2019.9

Language：English   Presentation type：Poster presentation  

Country：Japan  

Event date： 2019.7

Language：English   Presentation type：Poster presentation  

Country：Spain  

Event date： 2018.12

Language：English   Presentation type：Oral presentation (invited, special)  

Venue：Nanjing University   Country：Japan  

Event date： 2018.9

Language：English   Presentation type：Oral presentation (general)  

Venue：Okayama University   Country：Japan  

Event date： 2016.3

Language：Japanese   Presentation type：Oral presentation (invited, special)  

Venue：三重大学   Country：Japan  

Event date： 2015.9

Language：Japanese   Presentation type：Oral presentation (invited, special)  

Venue：岡崎コンファレンスセンター   Country：Japan  

Event date： 2015.6

Language：Japanese   Presentation type：Oral presentation (invited, special)  

Venue：東京大学駒場キャンパス   Country：Japan  

Event date： 2015.5

Language：English   Presentation type：Oral presentation (invited, special)  

Country：Japan  

Event date： 2015.3

Language：Japanese   Presentation type：Oral presentation (general)  

Country：Japan  

Event date： 2014.9

Language：Japanese   Presentation type：Oral presentation (general)  

Country：Japan  

Event date： 2014.7

Language：English   Presentation type：Oral presentation (invited, special)  

Country：Japan  

Event date： 2012.12

Language：Japanese   Presentation type：Oral presentation (invited, special)  

Venue：明星大学理工学部   Country：Japan  

Event date： 2012.6

Language：English   Presentation type：Oral presentation (invited, special)  

Country：China  

Event date： 2012.2

Language：Japanese   Presentation type：Oral presentation (invited, special)  

Venue：神戸大学統合研究拠点   Country：Japan  

Event date： 2011.9

Language：Japanese   Presentation type：Oral presentation (invited, special)  

Country：Japan  

Event date： 2011.7

Language：English   Presentation type：Poster presentation  

Country：Korea, Republic of  

Event date： 2011.7

Language：English   Presentation type：Oral presentation (invited, special)  

Country：Japan  

Event date： 2011.2

Language：English   Presentation type：Oral presentation (invited, special)  

Country：Korea, Republic of  

Event date： 2010.9

Language：Japanese   Presentation type：Oral presentation (invited, special)  

Venue：名古屋大学 ベンチャービジネスラボラトリー ベンチャーホール   Country：Japan  

タンパク質が熱揺らぎで構造転移をすることが、最近の一分子測定やNMRなどの実験からわかってきた。われわれは、構造転移を記述しうる粗視化モデル相互作用として、局所的相互作用がその周囲の変化に合わせて変化すると仮定するカメレオンモデルを提唱している。このモデルをアデニル酸キナーゼに対して適用した結果、実験で観測された二状態的な構造転移が再現されるとともに、モデルで計算された構造転移速度の温度変化が実測された酵素反応速度の温度変化とよく対応することがわかった。これらの結果は、カメレオンモデルが構造転移の

Event date： 2010.6

Language：Japanese   Presentation type：Oral presentation (invited, special)  

Country：Japan  

タンパク質がリガンド結合に伴い構造を変えることは長い間知られてきたが、近年は一定条件のもとで熱揺らぎで起こる構造転移に対しても、一分子実験やNMRなどによる実験的な特徴づけが進んできた。理論的立場からは、フォールディング研究における郷モデルの延長として、二つの結晶構造をともにエネルギー的に安定化する実効的相互作用が提唱されてきたが、二状態的な自由エネルギーランドスケープが得られるということ以上には実験事実との対応付けは行われていない。われわれはそれらの研究とは異なり、局所的相互作用がその周囲の変化

Event date： 2009.10

Language：Japanese   Presentation type：Oral presentation (invited, special)  

Country：Japan  

Event date： 2007.12

Language：Japanese   Presentation type：Poster presentation  

Country：Japan  

We have simulated the motion of myosin head along the actin filament with coarse-grained molecular dynamics with introduceing the sequence-dependent water-mediated potential. This potential have three variants depending on the degree of unfolding of each protein prior to binding. The simulation with this potential elucidates the contribution of hydrophobic and electrostatic interactions in the biased motion as well as the importance of coupled folding and binding.

Event date： 2007.11

Language：Japanese   Presentation type：Oral presentation (invited, special)  

Country：Japan  

ミオシン頭部の一方向的な滑り運動についての粗視化モデルを用いた分子動力学計算、および、カメレオンGoモデルによるアロステリック転移の分子動力学計算について

Event date： 2006.12

Language：English   Presentation type：Oral presentation (invited, special)  

Country：Japan  

Event date： 2006.11

Language：English   Presentation type：Poster presentation  

Country：Japan  

Event date： 2005.12

Language：Japanese   Presentation type：Oral presentation (general)  

Venue：東京大学山上会館   Country：Japan  

Event date： 2005.11

Language：Japanese   Presentation type：Poster presentation  

Country：Japan  

Event date： 2005.6

Language：Japanese   Presentation type：Oral presentation (invited, special)  

Country：Japan  

Event date： 2004.12

Language：Japanese   Presentation type：Poster presentation  

Country：Japan  

Event date： 2003.9

Language：Japanese   Presentation type：Poster presentation  

Country：Japan  

Event date： 2003.9

Language：Japanese   Presentation type：Oral presentation (invited, special)  

Country：Japan  

Event date： 2003.6

Language：Japanese   Presentation type：Oral presentation (invited, special)  

Country：Japan  

Event date： 2002.11

Language：English   Presentation type：Oral presentation (invited, special)  

Country：Japan  

Event date： 2002.8

Language：English   Presentation type：Poster presentation  

Event date： 2002.6

Language：Japanese   Presentation type：Poster presentation  

Country：Japan  

物理学における様々な問題を計算機を用いて調べる基本的な手法を学び，演習を通じて，応用する能力を身に着ける。

量子力学B、統計力学Bの演習を行う。

物質の微視的な性質と巨視的な性質を結びつける学問体系である統計力学の基礎的概念を、統計力学Aに続いて量子統計力学の導入およびそのいくつかの典型的な応用例を取り扱うことにより学ぶ。

物性科学や計算科学における基礎および最新の問題をとりあげて、発表、討論を通じて物理学と現代の科学技術との関わりについて理解を深める。創造力、表現力及び討論する力を学ぶ。

物理学における様々な問題を計算機を用いて調べる基本的な手法を学び，演習を通じて，応用する能力を身に着ける。

量子力学B、統計力学Bの演習を行う。

物質の微視的な性質と巨視的な性質を結びつける学問体系である統計力学の基礎的概念を、統計力学Aに続いて量子統計力学の導入およびそのいくつかの典型的な応用例を取り扱うことにより学ぶ。

タンパク質科学において計算科学がいかに用いられているかの実例を通して、 理論・計算生物物理学の基礎について講義する。

物性科学や計算科学における基礎および最新の問題をとりあげて、発表、討論を通じて物理学と現代の科学技術との関わりについて理解を深める。創造力、表現力及び討論する力を学ぶ。

物理学における様々な問題を計算機を用いて調べる基本的な手法を学び，演習を通じて，応用する能力を身に着ける。

量子力学B、統計力学Bの演習を行う。

物質の微視的な性質と巨視的な性質を結びつける学問体系である統計力学の基礎的概念を、統計力学Aに続いて量子統計力学の導入およびそのいくつかの典型的な応用例を取り扱うことにより学ぶ。

量子力学B、統計力学Bの演習を行う。

物性科学や計算科学における基礎および最新の問題をとりあげて、発表、討論を通じて物理学と現代の科学技術との関わりについて理解を深める。創造力、表現力及び討論する力を学ぶ。

タンパク質科学において計算科学がいかに用いられているかの実例を通して、
理論・計算生物物理学の基礎について講義する。

物質の微視的な性質と巨視的な性質を結びつける学問体系である統計力学の基礎的概念を、統計力学Aに続いて量子統計力学の導入およびそのいくつかの典型的な応用例を取り扱うことにより学ぶ。

物性科学や計算科学における基礎および最新の問題をとりあげて、発表、討論を通じて物理学と現代の科学技術との関わりについて理解を深める。創造力、表現力及び討論する力を学ぶ。