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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-...
Gorde:
| Argitaratua izan da: | Proc Jpn Acad Ser B Phys Biol Sci |
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| Egile nagusia: | |
| Formatua: | Artigo |
| Hizkuntza: | Inglês |
| Argitaratua: |
The Japan Academy
2017
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| Gaiak: | |
| Sarrera elektronikoa: | 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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