Nuclear magnetic resonance approaches for characterizing interactions between the bacterial chaperonin GroEL and unstructured proteins(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
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概要
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GroEL-protein interactions were characterized by stable isotope-assisted nuclear magnetic resonance (NMR) spectroscopy using chemically denatured bovine rhodanese and an intrinsically disordered protein, α-synuclein, as model ligands. NMR data indicated that proteins tethered to GroEL remain largely unfolded and highly mobile, enabling identification of the interaction hot spots displayed on intrinsically disordered proteins.
- 公益社団法人日本生物工学会の論文
著者
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Shimada Ichio
Graduate School Of Pharmaceutical Sciences The University Of Tokyo
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Yoshida Masasuke
Department Of Biochemistry Faculty Of Medicine Jichi Medical School
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Nishida Noritaka
Graduate School Of Pharmaceutical Sciences The University Of Tokyo
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Kato Koichi
Graduate School Of Natural Sciences Nagoya City University
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Motojima Fumihiro
Department of Molecular Biosciences, Faculty of Life Sciences, Kyoto Sangyo University
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Yagi-Utsumi Maho
Graduate School of Pharmaceutical Sciences, Nagoya City University:Institute for Molecular Science and Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences
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Nishida Noritaka
Graduate School of Pharmaceutical Sciences, The University of Tokyo:Graduate School of Pharmaceutical Sciences, Nagoya City University
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- 「多次元HPLCマップ法」の特集にあたって
- Nuclear magnetic resonance approaches for characterizing interactions between the bacterial chaperonin GroEL and unstructured proteins(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
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