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Title: Expanding heme-protein folding space using designed multi-heme β-sheet mini-proteins
Authors: D’Souza, Areetha
Torres, Jaume
Bhattacharjya, Surajit
Keywords: Biophysical Chemistry
Solution-state NMR
Science::Biological sciences
Issue Date: 2018
Source: D’Souza, A., Torres, J., & Bhattacharjya, S. (2018). Expanding heme-protein folding space using designed multi-heme β-sheet mini-proteins. Communications Chemistry, 1, 78-. doi:10.1038/s42004-018-0078-z
Series/Report no.: Communications Chemistry
Abstract: Nature has primarily exploited helical proteins, over β-sheets, for heme/multi-heme coordination. Understating of heme–protein structures has motivated the design of heme proteins utilizing coiled-coil helical structure. By contrast, de novo designed β-sheet proteins are less successful. However, designing proteins with discretely folded β-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 β-sheet mini-proteins (<40 amino acids) and proteins. Atomic-resolution structures demonstrate an expected β-sheet structural topology. The designed β-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 β-sheet heme proteins could serve as a platform for the generation of novel synthetic β-sheet protein mimics.
DOI: 10.1038/s42004-018-0078-z
Schools: School of Biological Sciences 
Rights: © 2018 The Author(s). This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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