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The kinetic and equilibrium molten globule intermediates of apoleghemoglobin differ in structure

An important question in protein folding is whether molten globule states formed under equilibrium conditions are good structural models for kinetic folding intermediates. The structures of the kinetic and equilibrium intermediates in the folding of the plant globin apoleghemoglobin have been compar...

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Библиографические подробности
Главные авторы: Nishimura, Chiaki, Dyson, H. Jane, Wright, Peter E.
Формат: Artigo
Язык:Inglês
Опубликовано: 2008
Предметы:
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC2409369/
https://ncbi.nlm.nih.gov/pubmed/18384808
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2008.03.025
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