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Dynamics of equilibrium structural fluctuations of apomyoglobin measured by fluorescence correlation spectroscopy

The spectra of equilibrium chain conformation fluctuations of apomyoglobin (apoMb) as a function of folding, from the acid-denatured state at pH 2.6 through the stable molten globule state pH ≈ 4.1 to the folded state at pH 6.3, are reported, as measured by fluorescence correlation spectroscopy. The...

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Bibliografski detalji
Glavni autori: Chen, Huimin, Rhoades, Elizabeth, Butler, James S., Loh, Stewart N., Webb, Watt W.
Format: Artigo
Jezik:Inglês
Izdano: National Academy of Sciences 2007
Teme:
Online pristup:https://ncbi.nlm.nih.gov/pmc/articles/PMC1965535/
https://ncbi.nlm.nih.gov/pubmed/17556539
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0704073104
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