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Protein-like fully reversible tetramerisation and super-association of an aminocellulose

Nikolajski, Melanie; Adams, Gary G.; Gillis, Richard B.; Besong, David Tabot; Rowe, Arthur J.; Heinze, Thomas; Harding, Stephen E.

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Authors

Melanie Nikolajski

Gary G. Adams

Richard B. Gillis

David Tabot Besong

Arthur J. Rowe

Thomas Heinze

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STEPHEN HARDING STEVE.HARDING@NOTTINGHAM.AC.UK
Professor of Applied Biochemistry



Abstract

Unusual protein-like, partially reversible associative behaviour has recently been observed in solutions of the water soluble carbohydrates known as 6-deoxy-6-(?-aminoalkyl)aminocelluloses, which produce controllable self-assembling films for enzyme immobilisation and other biotechnological applications. Now, for the first time, we have found a fully reversible self-association (tetramerisation) within this family of polysaccharides. Remarkably these carbohydrate tetramers are then seen to associate further in a regular way into supra-molecular complexes. Fully reversible oligomerisation has been hitherto completely unknown for carbohydrates and instead resembles in some respects the assembly of polypeptides and proteins like haemoglobin and its sickle cell mutation. Our traditional perceptions as to what might be considered "protein-like" and what might be considered as "carbohydrate-like" behaviour may need to be rendered more flexible, at least as far as interaction phenomena are concerned.

Citation

Nikolajski, M., Adams, G. G., Gillis, R. B., Besong, D. T., Rowe, A. J., Heinze, T., & Harding, S. E. (2014). Protein-like fully reversible tetramerisation and super-association of an aminocellulose. Scientific Reports, 4, Article 3861. https://doi.org/10.1038/srep03861

Journal Article Type Article
Acceptance Date Jan 6, 2014
Online Publication Date Jan 24, 2014
Publication Date Jan 24, 2014
Deposit Date Apr 4, 2017
Publicly Available Date Apr 4, 2017
Journal Scientific Reports
Electronic ISSN 2045-2322
Publisher Nature Publishing Group
Peer Reviewed Peer Reviewed
Volume 4
Article Number 3861
DOI https://doi.org/10.1038/srep03861
Public URL https://nottingham-repository.worktribe.com/output/721151
Publisher URL https://www.nature.com/articles/srep03861

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