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Makabe, Koki,Nakamura, Takashi,Dhar, Debanjan,Ikura, Teikichi,Koide, Shohei,Kuwajima, Kunihiro Elsevier 2018 Journal of molecular biology Vol.430 No.12
<P><B>Abstract</B></P> <P>Although many naturally occurring proteins consist of multiple domains, most studies on protein folding to date deal with single-domain proteins or isolated domains of multi-domain proteins. Studies of multi-domain protein folding are required for further advancing our understanding of protein folding mechanisms. <I>Borrelia</I> outer surface protein A (OspA) is a β-rich two-domain protein, in which two globular domains are connected by a rigid and stable single-layer β-sheet. Thus, OspA is particularly suited as a model system for studying the interplays of domains in protein folding. Here, we studied the equilibria and kinetics of the urea-induced folding–unfolding reactions of OspA probed with tryptophan fluorescence and ultraviolet circular dichroism. Global analysis of the experimental data revealed compelling lines of evidence for accumulation of an on-pathway intermediate during kinetic refolding and for the identity between the kinetic intermediate and a previously described equilibrium unfolding intermediate. The results suggest that the intermediate has the fully native structure in the N-terminal domain and the single layer β-sheet, with the C-terminal domain still unfolded. The observation of the productive on-pathway folding intermediate clearly indicates substantial interactions between the two domains mediated by the single-layer β-sheet. We propose that a rigid and stable intervening region between two domains creates an overlap between two folding units and can energetically couple their folding reactions.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Elucidation of mechanisms of multi-domain protein folding is an important issue. </LI> <LI> A two-domain protein OspA is a useful model for studying the multi-domain folding. </LI> <LI> We show evidence for the presence of an on-pathway folding intermediate in OspA. </LI> <LI> A rigid and stable intervening region between the domains played a critical role. </LI> <LI> The presence of such a region can lead to coupled folding behavior of the domains. </LI> </UL> </P> <P><B>Graphical abstract</B></P> <P>[DISPLAY OMISSION]</P>
On the Strichartz estimates for orthonormal systems of initial data with regularity
Bez, Neal,Hong, Younghun,Lee, Sanghyuk,Nakamura, Shohei,Sawano, Yoshihiro Elsevier 2019 Advances in Mathematics Vol.354 No.-
<P><B>Abstract</B></P> <P>The classical Strichartz estimates for the free Schrödinger propagator have recently been substantially generalised to estimates of the form [FORMULA OMISSION] for orthonormal systems <SUB> ( <SUB> f j </SUB> ) j </SUB> of initial data in <SUP> L 2 </SUP> , firstly in work of Frank–Lewin–Lieb–Seiringer and later by Frank–Sabin. The primary objective is identifying the largest possible <I>α</I> as a function of <I>p</I> and <I>q</I>, and in contrast to the classical case, for such estimates the critical case turns out to be ( p , q ) = ( d + 1 d , d + 1 d − 1 ) . We consider the case of orthonormal systems <SUB> ( <SUB> f j </SUB> ) j </SUB> in the homogeneous Sobolev spaces <SUP> H ˙ s </SUP> for s ∈ ( 0 , d 2 ) and we establish the sharp value of <I>α</I> as a function of <I>p</I>, <I>q</I> and <I>s</I>, except possibly an endpoint in certain cases. Furthermore, at the critical case ( p , q ) = ( d + 1 d − 2 s , d ( d + 1 ) ( d − 1 ) ( d − 2 s ) ) for general <I>s</I>, we show the veracity of the desired estimates when α = p if we consider frequency localised estimates, and the failure of the (non-localised) estimates when α = p ; this exhibits the difficulty of upgrading from frequency localised estimates in this context, again in contrast to the classical setting.</P>
Suda, Shoya,Ishibashi, Kenji,Riyana, Eka Sapta,Aida, Yani Nur,Nakamura, Shohei,Imahayashi, Yoichi The Korean Association for Radiation Protection 2016 방사선방어학회지 Vol.41 No.4
Background: Experiments with small electrochemical apparatus were previously carried out for detecting low-energy neutrinos under irradiation of reactor neutrinos and under natural neutrino environment. The experimental result indicated that the output current of reactor-neutrino irradiated detector was appreciably larger than that of natural environmental one. Usual interaction cross-sections of neutrinos are quite small, so that they do not explain the experimental result at all. Materials and Methods: To understand the experimental data, we propose that some biological products may generate AV-type scalar field B0, leading to a large interaction cross-section. The output current generation is ascribed to an electrochemical process that may be assisted by weak interaction phenomena. Dissolved oxygen concentrations in the detector solution were measured in this study, for the purpose of understanding the mechanism of the detector output current generation. Results and Discussion: It was found that the time evolution of experimental output current was mostly reproduced in simulation calculation on the basis of the measured dissolved oxygen concentration. Conclusion: We mostly explained the variation of experimental data by using the electrochemical half-cell analysis model based on the DO concentration that is consistent to the experiment.