Recent advances in the analysis of macromolecular interactions using the matrix-free method of sedimentation in the analytical ultracentrifugeTools 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 Full text not available from this repository.
Official URL: http://www.mdpi.com/2079-7737/4/1/237
AbstractSedimentation 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.
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