Melanie Nikolajski
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.
Authors
Gary G. Adams
Richard B. Gillis
David Tabot Besong
Arthur J. Rowe
Thomas Heinze
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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Copyright Statement
Copyright information regarding this work can be found at the following address: http://creativecommons.org/licenses/by/4.0
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