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- W2053820507 abstract "p97/Cdc48p/VCP is a highly conserved, essential member of the class of AAA+ ATPases present in both archaea and the eukaryotic cytosol. Like many of the AAA+ proteins, the functional state of p97 is a hexameric ring-shaped structure. However, the detailed relationship between monomer folding and assembly of the quaternary structure of p97, as well as other members of this class, has remained elusive. Here, we present a study of the structural changes of p97 during its folding and assembly, utilizing biophysical techniques including single-molecule Forster Resonance Energy Transfer (smFRET). p97 is large for using standard techniques to dual label with dyes for FRET studies. Therefore, this work aims to gain a deeper understanding about critical structural aspects of p97, while exploring advanced labeling methods that extend the scope of fluorescence studies to larger and more complex protein systems." @default.
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- W2053820507 date "2014-01-01" @default.
- W2053820507 modified "2023-09-26" @default.
- W2053820507 title "Single-Molecule and Ensemble Structural Study of the AAA+ Atpase P97" @default.
- W2053820507 doi "https://doi.org/10.1016/j.bpj.2013.11.351" @default.
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