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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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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
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The Japan Academy
2017
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| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5406622/ https://www.ncbi.nlm.nih.gov/pubmed/28077807 http://dx.doi.org/10.2183/pjab.93.002 |