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Recent advances in the analysis of macromolecular interactions using the matrix-free method of sedimentation in the analytical ultracentrifuge

Harding, Stephen; Gillis, Richard; Almutairi, Fahad; Erten, Tayyibe; K�k, M.; Adams, Gary

Recent advances in the analysis of macromolecular interactions using the matrix-free method of sedimentation in the analytical ultracentrifuge Thumbnail


Authors

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

Richard Gillis

Fahad Almutairi

Tayyibe Erten

M. K�k



Abstract

Sedimentation in the analytical ultracentrifuge is a matrix free solution technique with no immobilisation, columns, or membranes required and can be used to study self-association and complex or “hetero”-interactions, stoichiometry, reversibility and interaction strength of a wide variety of macromolecular types and across a very large dynamic range (dissociation constants from 10−12 M to 10−1 M). We extend an earlier review specifically highlighting advances in sedimentation velocity and sedimentation equilibrium in the analytical ultracentrifuge applied to protein interactions and mucoadhesion and to review recent applications in protein self-association (tetanus toxoid, agrin), protein-like carbohydrate association (aminocelluloses), carbohydrate-protein interactions (polysaccharide-gliadin), nucleic-acid protein (G-duplexes), nucleic acid-carbohydrate (DNA-chitosan) and finally carbohydrate-carbohydrate (xanthan-chitosan and a ternary polysaccharide complex) interactions.

Citation

Harding, S., Gillis, R., Almutairi, F., Erten, T., Kök, M., & Adams, G. (2015). Recent advances in the analysis of macromolecular interactions using the matrix-free method of sedimentation in the analytical ultracentrifuge. Biology, 4(1), https://doi.org/10.3390/biology4010237

Journal Article Type Article
Acceptance Date Feb 16, 2015
Publication Date Mar 6, 2015
Deposit Date Apr 3, 2017
Publicly Available Date Apr 3, 2017
Journal Biology
Electronic ISSN 2079-7737
Publisher MDPI
Peer Reviewed Peer Reviewed
Volume 4
Issue 1
DOI https://doi.org/10.3390/biology4010237
Keywords protein; carbohydrate; nucleic acid; interaction; hydrodynamics
Public URL https://nottingham-repository.worktribe.com/output/748009
Publisher URL http://www.mdpi.com/2079-7737/4/1/237

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