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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-...

Deskribapen osoa

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Xehetasun bibliografikoak
Argitaratua izan da:Proc Jpn Acad Ser B Phys Biol Sci
Egile nagusia: NISHIMURA, Chiaki
Formatua: Artigo
Hizkuntza:Inglês
Argitaratua: The Japan Academy 2017
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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