A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures

The yeast prion protein Sup35 is a translation termination factor, whose activity is modulated by sequestration into a self-perpetuating amyloid. The prion-determining domain, NM, consists of two distinct regions: an amyloidogenic N terminus domain (N) and a charged solubilizing middle region (M). T...

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Bibliographic Details
Main Authors: Mukhopadhyay, Samrat, Krishnan, Rajaraman, Lemke, Edward A., Lindquist, Susan, Deniz, Ashok A.
Format: Artigo
Language:Inglês
Published: National Academy of Sciences 2007
Subjects:
Biological Sciences
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC1815236/
https://ncbi.nlm.nih.gov/pubmed/17299036
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0611503104
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