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Thermodynamic stability of bacteriorhodopsin mutants measured relative to the bacterioopsin unfolded state

The stability of bacteriorhodopsin (bR) has often been assessed using SDS unfolding assays that monitor the transition of folded bR (bR(f)) to unfolded (bR(u)). While many criteria suggest that the unfolding curves reflect thermodynamic stability, slow retinal (RET) hydrolysis during refolding makes...

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Main Authors: Cao, Zheng, Schlebach, Jonathan, Park, Chiwook, Bowie, James U.
Formato: Artigo
Idioma:Inglês
Publicado: 2011
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Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC3272320/
https://ncbi.nlm.nih.gov/pubmed/21880269
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bbamem.2011.08.019
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