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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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Wedi'i Gadw mewn:
Manylion Llyfryddiaeth
Cyhoeddwyd yn:Proc Jpn Acad Ser B Phys Biol Sci
Prif Awdur: NISHIMURA, Chiaki
Fformat: Artigo
Iaith:Inglês
Cyhoeddwyd: The Japan Academy 2017
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
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