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Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin

Steady-state and transient conformational changes upon the thermal unfolding of ubiquitin were investigated with nonlinear IR spectroscopy of the amide I vibrations. Equilibrium temperature-dependent 2D IR spectroscopy reveals the unfolding of the β-sheet of ubiquitin through the loss of cross peaks...

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Bibliografische gegevens
Hoofdauteurs: Chung, Hoi Sung, Khalil, Munira, Smith, Adam W., Ganim, Ziad, Tokmakoff, Andrei
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: National Academy of Sciences 2005
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Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC545570/
https://ncbi.nlm.nih.gov/pubmed/15630083
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0408646102
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