Mahon, V., Fagan, R.P. and Smith, S.G. (2012) Snap denaturation reveals dimerization by AraC-like protein Rns. Biochimie, 94 (9). 2058 - 2061.
Abstract
Here we show that the Rns regulator of Escherichia coli dimerises in vivo and in vitro. Furthermore, we demonstrate that Rns forms aggregates in vitro and describe a methodology to ameliorate aggregation thus permitting the analysis of Rns by cross-linking.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2012 Elsevier. This is an author produced version of a paper subsequently published in Biochimie. Uploaded in accordance with the publisher's self-archiving policy. |
Keywords: | AraC Transcription Factor; Escherichia coli Proteins; Protein Denaturation; Protein Multimerization; Protein Structure, Quaternary; Recombinant Fusion Proteins; Trans-Activators |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield) > Department of Molecular Biology and Biotechnology (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 16 Apr 2014 13:32 |
Last Modified: | 23 Jun 2023 21:39 |
Published Version: | http://dx.doi.org/10.1016/j.biochi.2012.05.014 |
Status: | Published |
Publisher: | Elsevier |
Identification Number: | 10.1016/j.biochi.2012.05.014 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:78498 |