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D

D Pollard-Knight

Publications -  6
Citations -  855

D Pollard-Knight is an academic researcher. The author has contributed to research in topics: Gene & Surface plasmon resonance. The author has an hindex of 6, co-authored 6 publications receiving 849 citations.

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The Resonant Mirror: a novel optical biosensor for direct sensing of biomolecular interactions

TL;DR: The Resonant Mirror biosensor as mentioned in this paper uses the evanescent wave associated with a dielectric resonant structure to probe reactions occurring in a sensing layer, deposited within a few hundred nanometers of the device surface.
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The resonant mirror: a novel optical sensor for direct sensing of biomolecular interactions part II: applications

TL;DR: The broader applicability of the RM to studies on molecular interaction studies was demonstrated in an assay for the proteolytic enzyme trypsin and the specific inhibition of enzyme activity by α1-anti-trypsin.
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Kinetics of Protein-Protein Interactions at the Surface of an Optical Biosensor

TL;DR: It is suggested that steric hindrance caused by ligate binding to the dextran-coated sensor surface seems the most likely explanation for the observed biphasic association kinetics and that the faster initial phase should be used in oder to determine association constants that can be compared to those in solution.

Real-time Biomolecular Interaction Analysis Using the Resonant Mirror

TL;DR: The resonant mirror as discussed by the authors is a planar waveguide optical sensor that uses frustrated total internal reflection to couple light in and out of the waveguide layer, which is used as a biosensor to detect the highly selective binding interactions between pairs of biomolecules such as enzyme-substrate, antibody-antigen, hormone-receptor and DNA-DNA (DNA = deoxyribonucleic acid).
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Expression and characterisation of a protein specified by a synthetic horseradish peroxidase gene inEscherichia coli

TL;DR: A 940-bp gene specifying horseradish peroxidase isoenzyme C has been synthesised and expressed in bacteria and western blot analysis showed the protein to be recognised by polyclonal antibodies raised against native HRP.