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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-...
Wedi'i Gadw mewn:
| Cyhoeddwyd yn: | Proc Jpn Acad Ser B Phys Biol Sci |
|---|---|
| Prif Awdur: | |
| Fformat: | Artigo |
| Iaith: | Inglês |
| Cyhoeddwyd: |
The Japan Academy
2017
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| Pynciau: | |
| Mynediad Ar-lein: | 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 |
| Tagiau: |
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