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Signatures of hydrophobic collapse in extended proteins captured with force spectroscopy

We unfold and extend single proteins at a high force and then linearly relax the force to probe their collapse mechanisms. We observe a large variability in the extent of their recoil. Although chain entropy makes a small contribution, we show that the observed variability results from hydrophobic i...

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Autors principals: Walther, Kirstin A., Gräter, Frauke, Dougan, Lorna, Badilla, Carmen L., Berne, Bruce J., Fernandez, Julio M.
Format: Artigo
Idioma:Inglês
Publicat: National Academy of Sciences 2007
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Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC1876547/
https://ncbi.nlm.nih.gov/pubmed/17470816
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0702179104
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