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Rebecca J. Green
Researcher at University of Reading
Publications - 59
Citations - 4398
Rebecca J. Green is an academic researcher from University of Reading. The author has contributed to research in topics: Adsorption & Isothermal titration calorimetry. The author has an hindex of 33, co-authored 57 publications receiving 4042 citations. Previous affiliations of Rebecca J. Green include University of Surrey & University of Manchester.
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Journal ArticleDOI
Interaction of Flavonoids with Bovine Serum Albumin: A Fluorescence Quenching Study
TL;DR: The data suggested that the association between flavonoids and BSA did not change molecular conformation of BSA and that hydrogen bonding, ionic, and hydrophobic interaction are equally important driving forces for protein-flavonoid association.
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Surface plasmon resonance analysis of dynamic biological interactions with biomaterials
Rebecca J. Green,Richard A. Frazier,Kevin M. Shakesheff,Martyn C. Davies,Clive J. Roberts,Saul J. B. Tendler +5 more
TL;DR: A review of the diversity of SPR analysis shows the broad range of techniques that are routinely used alongside SPR analysis, and particular emphasis is given to the use of SPR as a complimentary tool.
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Interactions of tea tannins and condensed tannins with proteins.
Richard A. Frazier,E.R. Deaville,Rebecca J. Green,Elisabetta Stringano,Ian Willoughby,John Plant,Irene Mueller-Harvey +6 more
TL;DR: Binding parameters for the interactions of four types of tannins with gelatin and bovine serum albumin have been determined from isothermal titration calorimetry data, and the interactions with proteins were exothermic and involved multiple binding sites on the protein.
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Surface plasmon resonance for real time in situ analysis of protein adsorption to polymer surfaces.
TL;DR: The adsorption of a range of plasma proteins to metal and polymer surfaces has been examined using surface plasmon resonance (SPR) using a model polystyrene film spun coated directly onto this substrate which confirmed the presence of a closely packed protein layer for all three protein systems.
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Probing protein-tannin interactions by isothermal titration microcalorimetry.
TL;DR: Calorimetry data indicate that protein-tannin interaction mechanisms are dependent upon the nature of the protein involved and the structure and flexibility of the tannins themselves alters the stoichiometry of the interaction, but does not appear to have any significant affect on the overall binding mechanism observed.