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Keywords:

  • amyloid;
  • molecular modeling;
  • oligomerization;
  • peptides;
  • single-molecule studies
Thumbnail image of graphical abstract

Gaining recognition: The structure of a previously unrecognized antiparallel dimer of rat islet amyloid polypeptide bound to anionic membrane nanodiscs was examined by using a combination of single-pair FRET and Rosetta model refinement. Models of the dimer showed a likely interface for lipid binding and suggest key interactions may also occur in the human isoform, thereby providing possible insights into fibril formation in type II diabetes.