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- 저자 : Kunihiro Kuwajima (검색결과 4 건)
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Kuwajima Kunihiro,Inobe Tomonao,Arai Munehito The Polymer Society of Korea 2006 Macromolecular Research Vol.14 No.2
This is a short review article of our recent studies on the ATP-induced, allosteric conformational transition of the chaperonin GroEL complex by solution X-ray scattering. We used synchrotron X-ray scattering with a two-dimensional, charge-coupled, device-based X-ray detector to study (1) the specificity of the chaperonin GroEL for its ligand that induced the allosteric transition, and (2) the identification of the allosteric transition of GroEL in its complicated kinetics induced by ATP. Due to the dramatically increased sensitivity of the X-ray scattering technique based on the use of the two dimensional X-ray detector and synchrotron radiation, different allosteric conformational states of GroEL populated under different conditions were clearly distinguished from each other. It was concluded that solution X-ray scattering is an extremely powerful tool for investigating the equilibrium and kinetics of cooperative conformational transitions of oligomeric protein complex, especially when combined with other spectroscopic techniques such as fluorescence spectroscopy.
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Kunihiro Kuwajima,Tomonao Inobe,Munehito Arai 한국고분자학회 2006 Macromolecular Research Vol.14 No.2
This is a short review article of our recent studies on the ATP-induced, allosteric conformational transition of the chaperonin GroEL complex by solution X-ray scattering. We used synchrotron X-ray scattering with a two-dimensional, charge-coupled, device-based X-ray detector to study (1) the specificity of the chaperonin GroEL for its ligand that induced the allosteric transition, and (2) the identification of the allosteric transition of GroEL in its complicated kinetics induced by ATP. Due to the dramatically increased sensitivity of the X-ray scattering technique based on the use of the two dimensional X-ray detector and synchrotron radiation, different allosteric conformational states of GroEL populated under different conditions were clearly distinguished from each other. It was concluded that solution X-ray scattering is an extremely powerful tool for investigating the equilibrium and kinetics of coop erative conformational transitions of oligomeric protein complex, especially when combined with other spectro scopic techniques such as fluorescence spectroscopy.
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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>
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