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, Kök, M. and Adams, Gary (2015) Recent advances in the analysis of macromolecular interactions using the matrix-free method of sedimentation in the analytical ultracentrifuge. Biology, 4 (1). pp. 237-250. ISSN 2079-7737

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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.

Item Type: Article
RIS ID: https://nottingham-repository.worktribe.com/output/748009
Keywords: protein; carbohydrate; nucleic acid; interaction; hydrodynamics
Schools/Departments: University of Nottingham, UK > Faculty of Science > School of Biosciences
Identification Number: https://doi.org/10.3390/biology4010237
Depositing User: Eprints, Support
Date Deposited: 03 Apr 2017 11:55
Last Modified: 04 May 2020 17:04
URI: https://eprints.nottingham.ac.uk/id/eprint/41717

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