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Folding of apomyoglobin: Analysis of transient intermediate structure during refolding using quick hydrogen deuterium exchange and NMR
The structures of apomyoglobin folding intermediates have been widely analyzed using physical chemistry methods including fluorescence, circular dichroism, small angle X-ray scattering, NMR, mass spectrometry, and rapid mixing. So far, at least two intermediates (on sub-millisecond- and millisecond-...
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| 出版年: | Proc Jpn Acad Ser B Phys Biol Sci |
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| 第一著者: | |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
The Japan Academy
2017
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5406622/ https://ncbi.nlm.nih.gov/pubmed/28077807 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.2183/pjab.93.002 |
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