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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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Pubblicato in:Proc Jpn Acad Ser B Phys Biol Sci
Autore principale: NISHIMURA, Chiaki
Natura: Artigo
Lingua:Inglês
Pubblicazione: The Japan Academy 2017
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Accesso online: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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