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The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques

We use single-molecule force spectroscopy to study the kinetics of unfolding of the small protein ubiquitin. Upon a step increase in the stretching force, a ubiquitin polyprotein extends in discrete steps of 20.3 ± 0.9 nm marking each unfolding event. An average of the time course of these unfolding...

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Pubblicato in:Proc Natl Acad Sci U S A
Autori principali: Schlierf, Michael, Li, Hongbin, Fernandez, Julio M.
Natura: Artigo
Lingua:Inglês
Pubblicazione: National Academy of Sciences 2004
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Accesso online:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC409913/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/15123816/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.0400033101
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