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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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Main Authors: Nishimura, Chiaki, Dyson, H. Jane, Wright, Peter E.
Formato: Artigo
Idioma:Inglês
Publicado: 2008
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Acceso en liña: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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