Probing the Non-Native H Helix Translocation in Apomyoglobin Folding Intermediates

[Image: see text] Apomyoglobin folds via sequential helical intermediates that are formed by rapid collapse of the A, B, G, and H helix regions. An equilibrium molten globule with a similar structure is formed near pH 4. Previous studies suggested that the folding intermediates are kinetically trapp...

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Detalles Bibliográficos
Autores principales: Aoto, Phillip C., Nishimura, Chiaki, Dyson, H. Jane, Wright, Peter E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2014
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4067146/
https://www.ncbi.nlm.nih.gov/pubmed/24857522
http://dx.doi.org/10.1021/bi500478m

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4067146/
https://www.ncbi.nlm.nih.gov/pubmed/24857522
http://dx.doi.org/10.1021/bi500478m

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