Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/89035
Title: Designability of Aromatic Interaction Networks at E. coli Bacterioferritin B-Type Channels
Authors: Zhang, Yu
Zhou, Jinhua
Ardejani, Maziar S.
Li, Xun
Wang, Fei
Orner, Brendan P.
Keywords: Ferritin
Nano-cage
Issue Date: 2017
Source: Zhang, Y., Zhou, J., Ardejani, M. S., Li, X., Wang, F., & Orner, B. P. (2017). Designability of Aromatic Interaction Networks at E. coli Bacterioferritin B-Type Channels. Molecules, 22(12), 2184-.
Series/Report no.: Molecules
Abstract: The bacterioferritin from E. coli (BFR), a maxi-ferritin made of 24 subunits, has been utilized as a model to study the fundamentals of protein folding and self-assembly. Through structural and computational analyses, two amino acid residues at the B-site interface of BFR were chosen to investigate the role they play in the self-assembly of nano-cage formation, and the possibility of building aromatic interaction networks at B-type protein–protein interfaces. Three mutants were designed, expressed, purified, and characterized using transmission electron microscopy, size exclusion chromatography, native gel electrophoresis, and temperature-dependent circular dichroism spectroscopy. All of the mutants fold into α-helical structures and possess lowered thermostability. The double mutant D132W/N34W was 12 °C less stable than the wild type, and was also the only mutant for which cage-like nanostructures could not be detected in the dried, surface-immobilized conditions of transmission electron microscopy. Two mutants—N34W and D132W/N34W—only formed dimers in solution, while mutant D132W favored the 24-mer even more robustly than the wild type, suggesting that we were successful in designing proteins with enhanced assembly properties. This investigation into the structure of this important class of proteins could help to understand the self-assembly of proteins in general.
URI: https://hdl.handle.net/10356/89035
http://hdl.handle.net/10220/44762
ISSN: 1420-3049
DOI: http://dx.doi.org/10.3390/molecules22122184
Rights: © 2017 by The Author(s). Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SPMS Journal Articles

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