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Basic information |
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Name |
Chiaki Nishimura |
Belonging department |
Department of Pharmaceutical Sciences,Faculty of Pharmaceutical Sciences |
Occupation name |
Professor |
researchmap researcher code |
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researchmap agency |
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Folding of apomyoglobin: Analysis of transient intermediate structure during refolding using quick hydrogen deuterium exchange
The structures of apomyoglobin folding intermediates have been analyzed using physical chemistry methods including fluorescence, circular dichroism, small angle X-ray scattering, NMR, mass spectrometry, and rapid mixing. At least two intermediates have been demonstrated for apomyoglobin folding. It revealed that the combination of pH-pulse labeling and NMR is a useful tool.
Proc. Jpn. Acad., Ser. B, 93, 10-27, 2017
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