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Enhanced picture of protein-folding intermediates using organic solvents in H/D exchange and quench-flow experiments

Hydrogen/deuterium exchange followed by trapping of the labeled species in the aprotic solvent DMSO has been used to elucidate structure in both the burst-phase molten globule-folding intermediate of apomyoglobin and in an equilibrium intermediate that models the kinetic intermediate. Precise estima...

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Bibliografiset tiedot
Päätekijät: Nishimura, Chiaki, Dyson, H. Jane, Wright, Peter E.
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: National Academy of Sciences 2005
Aiheet:
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC555694/
https://ncbi.nlm.nih.gov/pubmed/15769860
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0409538102
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