%0 Journal Article
%T Expanding heme-protein folding space using designed multi-heme ¦Â-sheet mini-proteins
%J -
%D 2018
%R https://doi.org/10.1038/s42004-018-0078-z
%X Nature has primarily exploited helical proteins, over ¦Â-sheets, for heme/multi-heme coordination. Understating of heme¨Cprotein structures has motivated the design of heme proteins utilizing coiled-coil helical structure. By contrast, de novo designed ¦Â-sheet proteins are less successful. However, designing proteins with discretely folded ¦Â-sheet structures encoding specific functions would have great potential for the development of new synthetic molecules e.g. enzymes, inhibitors. Here we report the design and characterization of multi-heme binding four-, six-, eight-, and twelve-stranded ¦Â-sheet mini-proteins (<40 amino acids) and proteins. Atomic-resolution structures demonstrate an expected ¦Â-sheet structural topology. The designed ¦Â-sheet mini-proteins pack or latch multiple hemes with high affnity in versatile orientations either by stacking or sideways, mimicking naturally occuring multi-heme protein conduits. The designed multi-stranded ¦Â-sheet heme proteins could serve as a platform for the generation of novel synthetic ¦Â-sheet protein mimics
%U https://www.nature.com/articles/s42004-018-0078-z