Abstract
Peptide TZ1C2 can populate two distinct orientations: a staggered (out-of-register) fibril and an aligned (in-register) coiled-coil trimer. The coordination of two cadmium ions induces a registry shift that results in a reversible transition between these structural forms. This process recapitulates the self-assembly mechanism of native protein fibrils in which a ligand binding event gates a reversible conformational transition between alternate forms of a folded peptide structure.
Original language | English |
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Pages (from-to) | 10278-10281 |
Number of pages | 4 |
Journal | Journal of the American Chemical Society |
Volume | 135 |
Issue number | 28 |
DOIs | |
State | Published - Jul 17 2013 |