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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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Hlavní autoři: Schlierf, Michael, Li, Hongbin, Fernandez, Julio M.
Médium: Artigo
Jazyk:Inglês
Vydáno: National Academy of Sciences 2004
Témata:
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC409913/
https://ncbi.nlm.nih.gov/pubmed/15123816
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0400033101
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